Relevant bibliographies by topics / Biochemistry|Inorganic chemistry

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Reports

Academic literature on the topic 'Biochemistry|Inorganic chemistry'

Author: Grafiati
Published: 9 July 2021
Last updated: 15 February 2022

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Journal articles on the topic "Biochemistry|Inorganic chemistry"

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Silva, André M. N., Tânia Moniz, Baltazar de Castro, and Maria Rangel. "Human transferrin: An inorganic biochemistry perspective." Coordination Chemistry Reviews 449 (December 2021): 214186. http://dx.doi.org/10.1016/j.ccr.2021.214186.

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Lappert, M. F. "The role of oxygen in chemistry and biochemistry (Studies in inorganic chemistry 33)." Journal of Organometallic Chemistry 353, no. 1 (September 1988): C19. http://dx.doi.org/10.1016/0022-328x(88)80313-9.

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Erasmus, Daniel J., Sharon E. Brewer, and Bruno Cinel. "Integrating bio-inorganic and analytical chemistry into an undergraduate biochemistry laboratory." Biochemistry and Molecular Biology Education 43, no. 2 (March 4, 2015): 121–25. http://dx.doi.org/10.1002/bmb.20865.

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Messori, Luigi, and Felix Kratz. "Transferrin: From Inorganic Biochemistry to Medicine." Metal-Based Drugs 1, no. 2-3 (January 1, 1994): 161–67. http://dx.doi.org/10.1155/mbd.1994.161.

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Transferrin is one of the key proteins of iron metabolism in mammalians. It is responsible for the transfer of the essential iron(III) ions through the biological fluids from absorption to storage and utilization sites. Moreover, transferrin is involved in the metabolism of other metal ions that are either trace or toxic elements. In recent years the crystal structure of transferrin has been solved at high resolution. This has allowed an extensive reinterpretation of the many spectroscopic studies carried out on this protein in the last decade as well as the elucidation of some interesting structure-function relationships. We review here recent progresses in transferrin biochemistry, particular focus being given to those aspects that are relevant from a medical point of view.
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Levinger, Nancy E., and Bharat Baruah. "Journal of inorganic biochemistry – Crans special issue." Journal of Inorganic Biochemistry 208 (July 2020): 111108. http://dx.doi.org/10.1016/j.jinorgbio.2020.111108.

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Powell, A. K. "Book Review: Inorganic Biochemistry of Iron Metabolism. (Ellis Horwood Series in Inorganic Chemistry). By R. R. Crichton." Angewandte Chemie International Edition in English 31, no. 7 (July 1992): 930. http://dx.doi.org/10.1002/anie.199209301.

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Wolfson, Adele J., Susan L. Rowland, Gwendolyn A. Lawrie, and Anthony H. Wright. "Student conceptions about energy transformations: progression from general chemistry to biochemistry." Chem. Educ. Res. Pract. 15, no. 2 (2014): 168–83. http://dx.doi.org/10.1039/c3rp00132f.

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Students commencing studies in biochemistry must transfer and build on concepts they learned in chemistry and biology classes. It is well established, however, that students have difficulties in transferring critical concepts from general chemistry courses; one key concept is “energy.” Most previous work on students' conception of energy has focused on their understanding of energy in the context of physics (including the idea of “work”) and/or their understanding of energy in classical physical and inorganic chemistry contexts (particularly Gibbs Free Energy changes, the second law of thermodynamics, and equilibrium under standard conditions within a closed system). For biochemistry, students must go beyond those basic thermodynamics concepts of work, standard energy changes, and closed systems, and instead they must consider what energy flow, use, and transformation mean in living, open, and dynamic systems. In this study we explored students' concepts about free energy and flow in biological chemical reactions and metabolic pathways by surveys and in-depth interviews. We worked with students in general chemistry classes and biochemistry courses in both an Australian and a US tertiary institution. We address three primary questions (i) What are the most common alternative conceptions held by students when they explain energy-related phenomena in biochemistry?, (ii) What information do students transfer from introductory chemistry and biology when they are asked to consider energy in a biological reaction or reaction pathway?, and (iii) How do students at varying levels of competence articulate their understandings of energy in pathways and biological reactions? The answers to these questions are used to build a preliminary learning progression for understanding “energy” in biochemistry. We also propose crucial elements of content knowledge that instructors could apply to help students better grasp this threshold concept in biochemistry.
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Childs, A. F. "Studies in inorganic chemistry 10. Phosphorus. An outline of its chemistry, biochemistry and technology (4th edition)." Endeavour 15, no. 1 (January 1991): 36–37. http://dx.doi.org/10.1016/0160-9327(91)90102-h.

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Ochiai, Ei-Ichiro. "Inorganic Biochemistry, An Introduction; 2nd Edition (Cowan, J. A.)." Journal of Chemical Education 76, no. 4 (April 1999): 474. http://dx.doi.org/10.1021/ed076p474.2.

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Williams, R. J. P. "My past and a future role for inorganic biochemistry." Journal of Inorganic Biochemistry 100, no. 12 (December 2006): 1908–24. http://dx.doi.org/10.1016/j.jinorgbio.2006.09.002.

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Dissertations / Theses on the topic "Biochemistry|Inorganic chemistry"

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Bihari, Shailja. "Bio-inorganic chemistry of manganese and titanium." Thesis, University of Edinburgh, 2002. http://hdl.handle.net/1842/9995.

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A wide range of metals are transported in the body by the protein transferrin, including both essential metal ions and probably also metals used in therapeutic agents. The metal binding sites on transferrin contain tyrosine, histidine and aspartate ligands. This thesis is concerned with studies of the essential metal ion manganese, and with titanium, which is used in anticancer agents. In order to aid the characterisation of Mn(III) and Ti(IV) transferrins, the Mn(III) and Ti(IV) complexes with the model ligand ethylenebis[(a-hydroxyphenyl)glycine](H₄EHPG) have been studied. The Mn(III) complexes rac-Na[Mn(EHPG)].3H₂0 (1) and rac,mesoNa[Mn(EHPG)].H₂0 (2), have been prepared and their X-ray crystal structures determined. Complex 1 contains N(S,S)C(R,R) configurations at the N and C stereogenic centres, whilst in the unit cell of complex 2 there are two independent molecules, 2a (mesa) and 2b (rac), with N(R,R)C(S,R) and N(R,R)C(S,S) configurations, respectively. Enantiomers of each complex are also present. The Mn(III) centres have Jahn-Teller-distorted octahedral geometry, with two long bonds and four short bonds. ¹H NMR spectra of these high-spin d⁴ paramagnetic complexes are reported. These complexes give rise to similar ligand (phenolate)-tometal charge-transfer bands as Mn(III)-transferrin. Dissociation of Mn(III) from EHPG occurs below pH 3.4. The Ti(IV) complex of rac-[Ti(EHPG)(H₂0)].1113H₂0 (3) has also been prepared and the X-ray crystal structure determined. All previously-reported crystalline racEHPG metal complexes contain N(S,S)C(R,R), or N(R,R)C(S,S) isomers, whereas 3 unexpectedly contains the N(S,S)C(S,S) and N(R,R)C(R,R) forms. 2D NMR studies indicate that 3 has a similar structure in solution to that in the solid state. A ligand (phenolate)-to-metal charge transfer band was observed at 386 nm, similar to that seen for Ti(IV)-transferrin. Ti(IV)EHPG was stable at pH values down to 1, however, the complex decomposed above pH 7. Mn(III)-transferrin complexes were prepared by air oxidation of Mn(II) in the presence of transferrin. The oxidation state of manganese bound to transferrin was Abstract confirmed by K edge EXAFS. Analysis of the EXAFS data revealed that the metal centre is also Jahn-Teller distorted but with four long bonds and two short bonds, i.e. an inverse distortion to that seen in the Mn(III)EHPG model complexes. Attempts to prepare other Mn(III) complexes which might be suitable for studies of Mn transfer to proteins are described and include cyclam and bicyclam as ligands. The crystal structure of [Mn(cyclam)Ch]Cl₂H₂0 was determined, and contained two long axial Mn-Cl bonds of 2.5249 Å. This complex was shown by electronic absorption spectroscopy to undergo a complicated series of reactions in aqueous solution. K edge EXAFS measurements suggested that at least one Cl ligand dissociated from the complex in aqueous solution. The hydrolysis was shown to be inhibited by the presence of fluoride.
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Mantri, Yogita. "Computational modeling of transition metals in medicinal chemistry realistic models to probe metal-biomolecule binding energetics /." [Bloomington, Ind.] : Indiana University, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3386701.

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Thesis (Ph.D.)--Indiana University, Dept. of Chemistry, 2009.
Title from PDF t.p. (viewed on Jul 22, 2010). Source: Dissertation Abstracts International, Volume: 70-12, Section: B, page: 7549. Adviser: Mu-Hyun Baik.
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Freeman, Thomas L. "Folding and redox-linked conformational switching of the Geobacter heme sensor GSU0935." Thesis, Dartmouth College, 2014. http://pqdtopen.proquest.com/#viewpdf?dispub=1550957.

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Heme-based redox sensors are implicated in a number of important physiological processes such as nitrogen fixation, aerotaxis, and control of circadian cycles. These proteins often rely on proper ligand switching for functional activation. It is unclear how a protein's conformation in many of these heme-based sensors affects ligation at the heme and vice versa. GSU0935, a methyl-accepting chemotaxis sensor protein from Geobacter sulfurreducens, contains a periplasmic binding domain (PBD) with a c-type heme. Previous reports indicated that the heme iron switches its axial ligands from water to Met60 upon heme reduction. The heme iron ligation in the GSU0935 PBD was investigated in chemically-denatured protein samples to characterize the relationship between protein conformation and heme ligation using UV-visible absorbance spectroscopy. A red shift in the Soret band of GSU0935 was linked to misligation by deprotonated His169 at physiological pH under denaturing conditions. Stopped-flow studies showed that protein refolding results in rapid dissociation of His169 to be replaced by His54 as the distal heme ligand. His54 misligation acts as a kinetic trap during protein refolding and slows the formation of the native water-ligated heme. These results suggest that the heme domain of GSU0935 has a highly flexible N-terminal region and an exposed heme environment, which may be important for sensory function.

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Zierden, Mark Robert. "Towards Understanding the Trafficking and Function of Iron and Titanium Ions in Organisms." Diss., Temple University Libraries, 2016. http://cdm16002.contentdm.oclc.org/cdm/ref/collection/p245801coll10/id/421398.

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Chemistry
Ph.D.
It is estimated that up to one third of all proteins are metalloproteins. These proteins have evolved to use the metals that are, or at least were at the time of their initial evolution, the most accessible. Some active centers of metalloenzymes resemble the structures of minerals presumed to be present in precipitates from hydrothermal solutions in the ocean billions of years ago. The metals in these proteins serve myriad purposes from structure to transport to catalysis. For these purposes organisms must find a way to incorporate, transport and possibly store the metal ions from the environment. Iron, among other metals, is used for all the before mentioned purposes but in oxic aqueous conditions is hydrolysis prone. Depending on its oxidation state iron is either insoluble or reacts to form reactive oxygen species and is dangerous to organisms. Organisms have thus evolved complex mechanisms to overcome the challenges of trafficking hydrolysis prone metals. This dissertation will focus on the study of the trafficking of hydrolysis prone iron and titanium by organisms, from metal selection to their use and storage. An examination of why metals are chosen, sequestration and transport of these metals, and use of the metals is presented. This research, as a whole, explores the cellular life cycle of hydrolysis prone metals. It is thought that the first uses of metals before their incorporation by organisms were at mineral surfaces. To this end it would be useful for the organism to be able to attach to the mineral surface. Rhodococcus ruber GIN-1 was isolated for its ability to selectively bind to TiO2 over other metal oxides. Biologically it could be advantageous to selectively bind to one mineral surface over another. The isolation and identification of these proteins are examined within. Rhodococcus ruber GIN-1 has also been found to produce a novel siderophore. The siderophore is not yet completely identified but falls into the class of catecholates. Once organisms begin to incorporate and use metals in proteins it would be useful to sequester and concentrate necessary metal ions that exist in low concentration in their environment. There are multiple organisms that are known to sequester high levels of titanium. One relatively unexplored family is that of Sabellidae or the feather duster worm. Organisms like this have been proposed as sentinel organisms to detect metal pollution in waters. In a model Sabellidae organism we have detected elevated levels of titanium, among other metals. After metal sequestration from the environment, intraorganism transport of the ions to where they are necessary becomes important. Higher organisms use the transferrin family of proteins to traffic iron. While the transferrin cycle has been studied in depth, the reduction mechanism has not been elucidated in detail. We use a monolobal transferrin, nicatransferrin, from the model organism Ciona intestinalis to explore this iron reduction mechanism of the transferrin cycle and find that nicatransferrin can reduce iron with no external reductant. This reduction occurs on the timescale expected for the transferrin cycle and occurs without an iron (II) chelator. The source of the reducing equivalent is unknown but nicatransferrin was measured to have reduced up to 2.5 equivalents of iron. Once transported to cells the metal ions can be put to use and incorporated into proteins or other structures. We examine the possible intentional use of titanium as a pigment in Eudistoma purpuropuntatum. The most abundant titanium sequesterer known is Eudistoma ritteri, who concentrates titanium up to 1500 ppm (dry weight). Eudistoma purpuropunctatum, a close relative of Eudistoma ritteri, displays an interesting purple color due to small granules in its tunic. We investigate the source of the purple color in these granules and the ability of the organism to sequester titanium, finding that it has titanium concentrations on par with Eudistoma ritteri. The metal ions that are not put to immediate use can be stored. Some metals exist in labile pools but due to iron’s reactivity it is necessary to store it where it cannot cause cellular damage. The iron storage protein ferritin is a cage-like polymer made up of 24 ferritin monomers. The monomers exist as either H-chain or L-chain and the 24-mer can be comprised of just one type of these monomers or a mixture thereof. The covalent dimerization of the human L-chain 24-mer has been observed and the cause of this dimerization explored. We do not find direct evidence of the covalent linkage but do identify regions of the protein most likely to participate in the dimerization.
Temple University--Theses
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Alexander, Jessica L. "Characterization of Catalytic Metallodrugs: Advances towards Novel Antibiotics." The Ohio State University, 2017. http://rave.ohiolink.edu/etdc/view?acc_num=osu1503313186810767.

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Sabo, Michael J. "Tapping mode analysis of lambda-DNA and carboplatin interactions." Thesis, Southern Illinois University at Edwardsville, 2015. http://pqdtopen.proquest.com/#viewpdf?dispub=1600964.

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The purpose of this research was to examine the complexation of carboplatin and λ-DNA via atomic force microscopy. This project had the challenge of getting the necessary resolution which lead to the need to examine and improve upon the experimental protocol. These resolution issues were fixed by eliminating contamination, and by developing more consistent means of DNA application. The carboplatin and DNA complexation was then able to be observed. Initial indications are consistent with expectations because the DNA appears to become more condensed over time but further examination is required.

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Di, Pasqua Anthony J. "Carboplatin Exploring mechanism of action and improved drug delivery 1. Role of carbonate in the mechanism of action of carboplatin 2. Cytotoxicity of mesoporous silica nanomaterials /." Related electronic resource: Current Research at SU : database of SU dissertations, recent titles available full text, 2008. http://wwwlib.umi.com/cr/syr/main.

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Joshi, Hemant K. "Synthetic, structural, spectroscopic and computational studies of metal-dithiolates as models for pyranopterindithiolate molybdenum and tungsten enzymes: Dithiolate folding effect." Diss., The University of Arizona, 2003. http://hdl.handle.net/10150/280480.

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Coordination by an axial oxo and an equatorial ene-dithiolate group is a salient feature of the active sites of the mononuclear pyranopterin Mo/W enzymes. Discrete mononuclear model complexes encompassing these features are important in understanding the metal-ligand interactions in these active sites. The compounds (Tp*)ME(S-S) (M = Mo, W; E = O, NO) and Cp₂M(S-S) (M = Ti, Mo, W) (where Tp* is hydrotris(3,5-dimethyl-1-pyrazolyl)borate, Cp is η⁵-cyclopentadienyl, S-S represents a generic ene-1,2-dithiolate ligand for example 1,2-benzenedithiolate and 3,6-dichloro-1,2-benzenedithiolate) provide access to three different electronic configurations of the metal, formally d¹, d² and d⁰, respectively. These compounds also allow the study of two metal, two axial ligand and two equatorial ene-dithiolate perturbations. X-ray crystallography, density functional theory and photoelectron spectroscopy are utilized to understand the metal-sulfur interaction in the above complexes. Subtle differences in the geometry of these compounds are observed, including the metal-dithiolate fold angle which is sensitive to the electronic occupation of the metal in-plane orbital. This orbital is presumably the "host" orbital to the electrons during catalysis. The work in this area has resulted in the development of a dithiolate-folding-effect. This effect relates to the experimental verification of the Lauher and Hoffmann bonding model for the metal-dithiolate interaction in these complexes. This "dithiolate-folding-effect" is proposed to account for the electronic buffering at the metal center. This effect may provide a regulatory mechanism for the metal-sulfur interactions and could be a factor in the electron transfer reactions that regenerate the active sites of molybdenum and tungsten enzymes. The structure and properties of these compounds are correlated with those of the enzyme active sites.
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Oram, Paul Daniel 1963. "The potentiometric determination of the formation constants of a novel class of macrocyclic polyaminocarboxylic acid ligands and the formation constants of the mercury(II)-glutathione complexes." Diss., The University of Arizona, 1996. http://hdl.handle.net/10150/290597.

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Potentiometric titrations were used to determine the thermodynamic formation constants of the complexes of newly synthesized macrocyclic polyaminocarboxylic acid ligands with selected metal ions. The formation constants were calculated with the help of a computer modeling program, BEST. Protonated complexes and hydroxylated complexes often coexist with the neutral complex in certain pH regions. This formation of multiple species is an important consideration in putting these ligands to practical use. It was also found that some of the complexes undergo a change in geometry when the pH of the solution is changed from acidic to basic. Electron spin resonance and UV-visible spectra confirmed these changes. The formation constants of the mercury(II)-glutathione complexes were also determined by potentiometric titrations. It was found that the previously reported value was incorrect by approximately ten orders of magnitude. The formation constants of the secondary species were also determined. These values have not been reported previously. A complete understanding of the solution chemistry of these complexes should be beneficial for understanding the metabolism of mercury(II) in living organisms.
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Williams, Wesley S. "Method development for long-term monitoring of heavy metals in mussel shells by laser-ablation inductively-coupled-plasma mass-spectrometry." Thesis, The University of Tulsa, 2014. http://pqdtopen.proquest.com/#viewpdf?dispub=3622730.

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Heavy metal pollution is a growing concern as growing worldwide population and industrial processes increase pollution levels in most environments. High metal concentrations throughout ecosystems pose a serious threat to wild-life and human health. Methods to monitor rising threat levels of metals are a primary concern for monitoring overall ecosystem health. Mechanisms which spread pollution must be intimately understood because of the persistence of heavy metals. Heavy metal contamination in the Tar Creek superfund site provides a great case study to selectively observe differences in heavy metals concentrations both upstream and downstream of mining activity. Thus, research is able to identify natural and man-made point sources of pollution.

The abilities of bivalves to filter-feed and sediment-feed provide a unique monitoring tool for analyzing heavy metals. Mussels are constantly filtering the environment around them. A mussel's seasonal and annual growth layers provide an excellent sample media for obtaining historical records of environmental data. Many species of mussels are found in most freshwater ecosystems throughout the United States. Mussels have low migration rates, live for a suitable amount of time, and leave relic shells. These features make mussels very practical for monitoring heavy metal pollution.

Various studies were conducted to obtain insight into developing methods for using LA-ICP-MS as a tool for monitoring heavy metals in mussel shells. Surface laser ablations, compared at additional depths, resulted in a more than 20% increase in signal intensity. Theoretical and experimental designs show signal changes as a function of depth. Mussel tissue and shell digestions were found to be best when using approximately 1.0 mL of hydrogen peroxide and 1.0 mL of nitric acid for each 0.1 grams of sample. Mussel tissue was found to have greater heavy metal concentrations than shells. Shells were found to average a 96% weight of calcium carbonate; however, the organic layers contained the greatest concentrations of heavy metals per weight.

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Books on the topic "Biochemistry|Inorganic chemistry"

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Inorganic biochemistry: An introduction. New York, N.Y: VCH, 1993.

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Inorganic biochemistry: An introduction. 2nd ed. New York: Wiley-VCH, 1997.

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Swart, Marcel, and Miquel Costas, eds. Spin States in Biochemistry and Inorganic Chemistry. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.

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B, Goodenough J., Ibers J. A, Jørgensen C. K, Mingos D. M. P, Neilands J. B, Palmer G. A, Reinen D, Sadler P. J, Weiss Ronald 1937-, and Williams R. J. P, eds. Bioinorganic Chemistry. Berlin, Heidelberg: Springer Berlin Heidelberg, 1988.

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J. J. R. Fraústo da Silva. The biological chemistry of the elements: The inorganic chemistry of life. Oxford: Clarendon Press, 1993.

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P, Williams R. J., ed. The biological chemistry of the elements: The inorganic chemistry of life. Oxford: Clarendon Press, 1997.

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Mingos, D. Michael P., ed. Nitrosyl Complexes in Inorganic Chemistry, Biochemistry and Medicine II. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-41160-1.

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Mingos, D. Michael P., ed. Nitrosyl Complexes in Inorganic Chemistry, Biochemistry and Medicine I. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-41187-8.

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Horovitz, Chaim T. Biochemistry of Scandium and Yttrium, Part 2: Biochemistry and Applications. Boston, MA: Springer US, 2000.

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Principles of general, organic, & biological chemistry. New York: McGraw-Hill, 2012.

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Book chapters on the topic "Biochemistry|Inorganic chemistry"

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Denisov, Ilia G. "Cryoradiolysis as a Method for Mechanistic Studies in Inorganic Biochemistry." In Physical Inorganic Chemistry, 109–42. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2010. http://dx.doi.org/10.1002/9780470602539.ch4.

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Usharani, Dandamudi, Binju Wang, Dina A. Sharon, and Sason Shaik. "Principles and Prospects of Spin-States Reactivity in Chemistry and Bioinorganic Chemistry." In Spin States in Biochemistry and Inorganic Chemistry, 131–56. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch7.

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Sanders, Brian C., Melody A. Rhine, and Todd C. Harrop. "Properties of {FeNO}8 and {CoNO}9 Metal Nitrosyls in Relation to Nitroxyl Coordination Chemistry." In Molecular Design in Inorganic Biochemistry, 57–88. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/430_2012_87.

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Papish, Elizabeth T., Natalie A. Dixon, and Mukesh Kumar. "Biomimetic Chemistry with Tris(triazolyl)borate Ligands: Unique Structures and Reactivity via Interactions with the Remote Nitrogens." In Molecular Design in Inorganic Biochemistry, 115–50. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/430_2012_86.

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Swart, Marcel, and Miquel Costas. "General Introduction to Spin States." In Spin States in Biochemistry and Inorganic Chemistry, 1–5. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch1.

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Cook, Sarah A., David C. Lacy, and Andy S. Borovik. "Terminal Metal-Oxo Species with Unusual Spin States." In Spin States in Biochemistry and Inorganic Chemistry, 203–27. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch10.

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Heims, Florian, and Kallol Ray. "Multiple Spin Scenarios in Transition-Metal Complexes Involving Redox Non-Innocent Ligands." In Spin States in Biochemistry and Inorganic Chemistry, 229–62. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch11.

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Aromí, Guillem, Patrick Gamez, and Olivier Roubeau. "Molecular Magnetism." In Spin States in Biochemistry and Inorganic Chemistry, 263–96. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch12.

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Hopmann, Kathrin H., Vladimir Pelmenschikov, Wen-Ge Han Du, and Louis Noodleman. "Electronic Structure, Bonding, Spin Coupling, and Energetics of Polynuclear Iron-Sulfur Clusters - A Broken Symmetry Density Functional Theory Perspective." In Spin States in Biochemistry and Inorganic Chemistry, 297–325. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch13.

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Petrenko, Alexander, and Matthias Stein. "Environment Effects on Spin States, Properties, and Dynamics from Multi-Level QM/MM Studies." In Spin States in Biochemistry and Inorganic Chemistry, 327–67. Oxford, UK: John Wiley & Sons, Ltd, 2015. http://dx.doi.org/10.1002/9781118898277.ch14.

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Reports on the topic "Biochemistry|Inorganic chemistry"

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Terah, Elena Igorevna. The work program, guidelines and evaluation materials of the discipline «Inorganic Chemistry» for students of the specialty «Medical Biochemistry». Novosibirsk State Medical University, 2020. http://dx.doi.org/10.12731/inorganicchemistry-terahelena.

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