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Journal articles on the topic 'Chromoproteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

Zein, N., P. Reiss, M. Bernatowicz, and M. Bolgar. "The proteolytic specificity of the natural enediyne-containing chromoproteins is unique to each chromoprotein." Chemistry & Biology 2, no. 7 (1995): 451–55. http://dx.doi.org/10.1016/1074-5521(95)90262-7.

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2

LYLE, PAUL A., and WALTER S. STRUVE. "DYNAMIC LINEAR DICHROISM IN CHROMOPROTEINS." Photochemistry and Photobiology 53, no. 3 (1991): 359–65. http://dx.doi.org/10.1111/j.1751-1097.1991.tb03641.x.

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3

Inoue, A., T. Yamashita, T. Horie, M. Ohkuma, M. Nakagawa, and M. Tsuda. "Light sensitive chromoproteins in octopus skin." Seibutsu Butsuri 40, supplement (2000): S34. http://dx.doi.org/10.2142/biophys.40.s34_2.

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4

Gafert, J., J. Friedrich, F. Parak, and J. Fidy. "Hole burning and pressure phenomena in chromoproteins." Journal of Luminescence 56, no. 1-6 (1993): 157–64. http://dx.doi.org/10.1016/0022-2313(93)90067-w.

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5

Shkrob, Maria A., Yurii G. Yanushevich, Dmitriy M. Chudakov, et al. "Far-red fluorescent proteins evolved from a blue chromoprotein from Actinia equina." Biochemical Journal 392, no. 3 (2005): 649–54. http://dx.doi.org/10.1042/bj20051314.

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Proteins of the GFP (green fluorescent protein) family demonstrate a great spectral and phylogenetic diversity. However, there is still an intense demand for red-shifted GFP-like proteins in both basic and applied science. To obtain GFP-like chromoproteins with red-shifted absorption, we performed a broad search in blue-coloured Anthozoa species. We revealed specimens of Actinia equina (beadlet anemone) exhibiting a bright blue circle band at the edge of the basal disc. A novel blue chromoprotein, aeCP597, with an absorption maximum at 597 nm determining the coloration of the anemone basal disk was cloned. AeCP597 carries a chromophore chemically identical with that of the well-studied DsRed (red fluorescent protein from Discosoma sp.). Thus a strong 42-nm bathochromic shift of aeCP597 absorption compared with DsRed is determined by peculiarities of chromophore environment. Site-directed and random mutagenesis of aeCP597 resulted in far-red fluorescent mutants with emission maxima at up to 663 nm. The most bright and stable mutant AQ143 possessed excitation and emission maxima at 595 and 655 nm respectively. Thus aeCP597 and its fluorescent mutants set a new record of red-shifted absorption and emission maxima among GFP-like proteins.

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6

Yamashita, T., A. Inoue, and M. Tsida. "Light sensitive chromoproteins in chromatophore of the Octopus." Seibutsu Butsuri 41, supplement (2001): S66. http://dx.doi.org/10.2142/biophys.41.s66_4.

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7

Timpmann, Kõu, Gediminas Trinkunas, John D. Olsen, C. Neil Hunter, and Arvi Freiberg. "Bandwidth of excitons in LH2 bacterial antenna chromoproteins." Chemical Physics Letters 398, no. 4-6 (2004): 384–88. http://dx.doi.org/10.1016/j.cplett.2004.09.090.

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8

Tamayo-Nuñez, Jessica, Javier de la Mora, Felipe Padilla-Vaca, et al. "aeBlue Chromoprotein Color is Temperature Dependent." Protein & Peptide Letters 27, no. 1 (2019): 74–84. http://dx.doi.org/10.2174/0929866526666190806145740.

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Background: Marine sessile organisms display a color palette that is the result of the expression of fluorescent and non-fluorescent proteins. Fluorescent proteins have uncovered transcriptional regulation, subcellular localization of proteins, and the fate of cells during development. Chromoproteins have received less attention until recent years as bioreporters. Here, we studied the properties of aeBlue, a a 25.91 kDa protein from the anemone Actinia equina. Objective: To assess the properties of aeBlue chromoprotein under different physicochemical conditions. Method: In this article, during the purification of aeBlue we uncovered that it suffered a color shift when frozen. We studied the color shift by different temperature incubation and physicochemical conditions and light spectroscopy. To assess the possible structural changes in the protein, circular dichroism analysis, size exclusion chromatography and native PAGE was performed. Results: We uncover that aeBlue chromoprotein, when expressed from a synthetic construct in Escherichia coli, showed a temperature dependent color shift. Protein purified at 4 °C by metal affinity chromatography exhibited a pinkish color and shifts back at higher temperatures to its intense blue color. Circular dichroism analysis revealed that the structure in the pink form of the protein has reduced secondary structure at 4 °C, but at 35 °C and higher, the structure shifts to a native conformation and Far UV- vis CD spectra revealed the shift in an aromatic residue of the chromophore. Also, the chromophore retains its properties in a wide range of conditions (pH, denaturants, reducing and oxidants agents). Quaternary structure is also maintained as a tetrameric conformation as shown by native gel and size exclusion chromatography. Conclusion: Our results suggest that the chromophore position in aeBlue is shifted from its native position rendering the pink color and the process to return it to its native blue conformation is temperature dependent.

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9

UNNO, Masashi. "Raman Optical Activity Probing the Active Site of Chromoproteins." Seibutsu Butsuri 54, no. 1 (2014): 039–42. http://dx.doi.org/10.2142/biophys.54.039.

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10

Kobachi, Kenju, Sota Kuno, Shinya Sato, Kenta Sumiyama, Michiyuki Matsuda, and Kenta Terai. "Biliverdin Reductase-A Deficiency Brighten and Sensitize Biliverdin-binding Chromoproteins." Cell Structure and Function 45, no. 2 (2020): 131–41. http://dx.doi.org/10.1247/csf.20010.

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11

Friedrich, J., J. Gafert, J. Zollfrank, J. Vanderkooi, and J. Fidy. "Spectral hole burning and selection of conformational substates in chromoproteins." Proceedings of the National Academy of Sciences 91, no. 3 (1994): 1029–33. http://dx.doi.org/10.1073/pnas.91.3.1029.

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12

Shkrob, M. A., A. S. Mishin, D. M. Chudakov, Yu A. Labas, and K. A. Lukyanov. "Chromoproteins of the green fluorescent protein family: Properties and applications." Russian Journal of Bioorganic Chemistry 34, no. 5 (2008): 517–25. http://dx.doi.org/10.1134/s1068162008050014.

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13

Verkhusha, Vladislav V., and Konstantin A. Lukyanov. "The molecular properties and applications of Anthozoa fluorescent proteins and chromoproteins." Nature Biotechnology 22, no. 3 (2004): 289–96. http://dx.doi.org/10.1038/nbt943.

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14

Chee, Ryan K. W., Yan Li, Wei Zhang, and Robert E. Campbell. "In vivo photoacoustic difference-spectra imaging of bacteria using photoswitchable chromoproteins." Journal of Biomedical Optics 23, no. 10 (2018): 1. http://dx.doi.org/10.1117/1.jbo.23.10.106006.

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15

Walsh, Susan Jennifer. "Genetics in Action: Mutation of Chromoproteins in First‐Semester Introductory Biology." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.07333.

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16

Gurskaya, Nadya G., Arkady F. Fradkov, Alexey Terskikh, et al. "GFP-like chromoproteins as a source of far-red fluorescent proteins." FEBS Letters 507, no. 1 (2001): 16–20. http://dx.doi.org/10.1016/s0014-5793(01)02930-1.

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17

Gafert, J., J. Friedrich, and F. Parak. "Stark-effect experiments on photochemical holes in chromoproteins: protoporphyrin IX-substituted myoglobin." Proceedings of the National Academy of Sciences 92, no. 6 (1995): 2116–20. http://dx.doi.org/10.1073/pnas.92.6.2116.

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18

Falk, H., N. M�ller, and M. Oberreiter. "Concerning the question of covalent bonding in hypericin-chromoproteins: Schiff base formation?" Monatshefte f�r Chemie Chemical Monthly 125, no. 3 (1994): 313–23. http://dx.doi.org/10.1007/bf00811317.

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19

Verkhusha, Vladislav V., Dmitry M. Chudakov, Nadya G. Gurskaya, Sergey Lukyanov, and Konstantin A. Lukyanov. "Common Pathway for the Red Chromophore Formation in Fluorescent Proteins and Chromoproteins." Chemistry & Biology 11, no. 6 (2004): 845–54. http://dx.doi.org/10.1016/j.chembiol.2004.04.007.

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20

Tafoya-Ramírez, Margarita, Felipe Padilla-Vaca, Ana Ramírez-Saldaña, et al. "Replacing Standard Reporters from Molecular Cloning Plasmids with Chromoproteins for Positive Clone Selection." Molecules 23, no. 6 (2018): 1328. http://dx.doi.org/10.3390/molecules23061328.

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21

Akashi, Takehiro, Maiko Okajima, and Tatsuo Kaneko. "Extraction of chromoproteins from Aphanothece sacrum and their applications to optically functional materials." Journal of Biotechnology 136 (October 2008): S450. http://dx.doi.org/10.1016/j.jbiotec.2008.07.1045.

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22

Battad, Jion M., Pascal G. Wilmann, Seth Olsen, et al. "A Structural Basis for the pH-dependent Increase in Fluorescence Efficiency of Chromoproteins." Journal of Molecular Biology 368, no. 4 (2007): 998–1010. http://dx.doi.org/10.1016/j.jmb.2007.02.007.

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23

Lei, Zhao, Yun Zeng, Xiaofen Zhang, Xiaoyong Wang, and Gang Liu. "Photoacoustic reporter genes for noninvasive molecular imaging and theranostics." Journal of Innovative Optical Health Sciences 13, no. 03 (2020): 2030005. http://dx.doi.org/10.1142/s1793545820300050.

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Noninvasive molecular imaging makes the observation and comprehensive understanding of complex biological processes possible. Photoacoustic imaging (PAI) is a fast evolving hybrid imaging technology enabling in vivo imaging with high sensitivity and spatial resolution in deep tissue. Among the various probes developed for PAI, genetically encoded reporters attracted increasing attention of researchers, which provide improved performance by acquiring images of a PAI reporter gene’s expression driven by disease-specific enhancers/promoters. Here, we present a brief overview of recent studies about the existing photoacoustic reporter genes (RGs) for noninvasive molecular imaging, such as the pigment enzyme reporters, fluorescent proteins and chromoproteins, photoswitchable proteins, including their properties and potential applications in theranostics. Furthermore, the challenges that PAI RGs face when applied to the clinical studies are also examined.

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24

Lambert, Gerard G., Hadrien Depernet, Guillaume Gotthard, et al. "Aequorea’s secrets revealed: New fluorescent proteins with unique properties for bioimaging and biosensing." PLOS Biology 18, no. 11 (2020): e3000936. http://dx.doi.org/10.1371/journal.pbio.3000936.

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Using mRNA sequencing and de novo transcriptome assembly, we identified, cloned, and characterized 9 previously undiscovered fluorescent protein (FP) homologs from Aequorea victoria and a related Aequorea species, with most sequences highly divergent from A. victoria green fluorescent protein (avGFP). Among these FPs are the brightest green fluorescent protein (GFP) homolog yet characterized and a reversibly photochromic FP that responds to UV and blue light. Beyond green emitters, Aequorea species express purple- and blue-pigmented chromoproteins (CPs) with absorbances ranging from green to far-red, including 2 that are photoconvertible. X-ray crystallography revealed that Aequorea CPs contain a chemically novel chromophore with an unexpected crosslink to the main polypeptide chain. Because of the unique attributes of several of these newly discovered FPs, we expect that Aequorea will, once again, give rise to an entirely new generation of useful probes for bioimaging and biosensing.

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25

Kangur, Liina, Margus Rätsep, Kõu Timpmann, Zheng-Yu Wang-Otomo, and Arvi Freiberg. "The two light-harvesting membrane chromoproteins of Thermochromatium tepidum expose distinct robustness against temperature and pressure." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1861, no. 8 (2020): 148205. http://dx.doi.org/10.1016/j.bbabio.2020.148205.

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26

Smith, E. G., C. D’Angelo, A. Salih, and J. Wiedenmann. "Screening by coral green fluorescent protein (GFP)-like chromoproteins supports a role in photoprotection of zooxanthellae." Coral Reefs 32, no. 2 (2013): 463–74. http://dx.doi.org/10.1007/s00338-012-0994-9.

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27

Brodhun, Bonita, and Donat-P. Häder. "A novel procedure to isolate the chromoproteins in the paraflagellar body of the flagellate Euglena gracilis." Journal of Photochemistry and Photobiology B: Biology 28, no. 1 (1995): 39–45. http://dx.doi.org/10.1016/1011-1344(94)07092-3.

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28

Semenova, Anna A., Evelina I. Nikelshparg, Nadezhda A. Brazhe, Irina A. Veselova, and Eugene A. Goodilin. "Nanoelements in Mendeleev’s Periodic Table. Copper Subgroup." Vestnik RFFI, no. 2 (June 25, 2019): 46–57. http://dx.doi.org/10.22204/2410-4639-2019-102-02-46-57.

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The 150th anniversary of the Mendeleev’s Periodic Table of elements requires scientists to rethink the outstanding role of this fundamental law in modern areas of chemistry, including such interdisciplinary and high-tech fields as nanochemistry and nanomaterials. The situation analysis shows that the most “nanotechnologically” popular elements belong to 1st, 2nd and partially to the 3rd periods, wherein a special practically important role is played by the noble metals because of their clear «specialization» in the development and implementation of new analytical techniques, in particular, the surface-enhanced Raman spectroscopy (SERS). There is an obvious need to develop and introduce fundamentally new, unique approaches and tools for the analysis of functioning living tissue structures. And SERS is precisely such a method, which implements multiplex, nonivasive spatially- and time-resolved control of chromoproteins at the extremely low concentrations in small volumes of samples of biological objects (tissues, cells, cell structures / organelles), and is an important innovative method of practical biomedical diagnostics.

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29

Heyd, Bernadette, Guilhem Lerat, Elisabeth Adjadj, Philippe Minard, and Michel Desmadril. "Reinvestigation of the Proteolytic Activity of Neocarzinostatin." Journal of Bacteriology 182, no. 7 (2000): 1812–18. http://dx.doi.org/10.1128/jb.182.7.1812-1818.2000.

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ABSTRACT Neocarzinostatin (NCS) is the most studied member of a family of chromoproteins secreted by a range of actinomycetes species. It has been proposed that in addition to their antitumoral activity related to the bound chromophores, this group of related proteins could be a secreted proteases superfamily. With the aim of dissecting the molecular basis of the proteolytic activity of NCS, an expression system allowing efficient expression of apo-NCS in Escherichia coli was constructed. The recombinant protein was properly folded and functional. Its histone-specific proteolytic activity was similar to the activity described for the natural protein. Further analyses unambiguously demonstrated that the proteolytic activity could be physically separated from NCS. This activity is therefore due not to NCS itself but to minor contaminating proteases, the nature of which differed in the recombinant and natural NCS preparations. The histone degradation test commonly used to monitor proteolytic activity is extremely sensitive and may easily generate false-positive results. These results strongly suggest that the possible proteolytic activity of the proteins of this family should be critically reconsidered.

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30

Remberg, Anja, Antje Ruddat, Silvia E. Braslavsky, Wolfgang Gärtner, and Kurt Schaffner. "Chromophore Incorporation, Prto PfrKinetics, and PfrThermal Reversion of Recombinant N-Terminal Fragments of Phytochrome A and B Chromoproteins‡." Biochemistry 37, no. 28 (1998): 9983–90. http://dx.doi.org/10.1021/bi980575x.

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31

HILL, Christiane, Wolfgang GARTNER, Paul TOWNER, Silvia E. BRASLAVSKY, and Kurt SCHAFFNER. "Expression of phytochrome apoprotein from Avena sativa in Escherichia coli and formation of photoactive chromoproteins by assembly with phycocyanobilin." European Journal of Biochemistry 223, no. 1 (1994): 69–77. http://dx.doi.org/10.1111/j.1432-1033.1994.tb18967.x.

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32

Telegina, T. A., M. V. Biryukov, I. V. Terekhova, Yu L. Vechtomova, and M. S. Kritsky. "Isolation and Characterization of Water-Soluble Chromoproteins from Arthrospira platensis Cyanobacteria: C-Phycocyanin, Allophycocyanin, and Carotenoid- and Chlorophyll-Binding Proteins." Applied Biochemistry and Microbiology 54, no. 6 (2018): 631–38. http://dx.doi.org/10.1134/s0003683818060145.

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33

Burgie, E. Sethe, Zachary T. K. Gannam, Katrice E. McLoughlin, et al. "Differing biophysical properties underpin the unique signaling potentials within the plant phytochrome photoreceptor families." Proceedings of the National Academy of Sciences 118, no. 22 (2021): e2105649118. http://dx.doi.org/10.1073/pnas.2105649118.

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Many aspects of photoperception by plants and microorganisms are initiated by the phytochrome (Phy) family of photoreceptors that detect light through interconversion between red light- (Pr) and far-red light-absorbing (Pfr) states. Plants synthesize a small family of Phy isoforms (PhyA to PhyE) that collectively regulate photomorphogenesis and temperature perception through redundant and unique actions. While the selective roles of these isoforms have been partially attributed to their differing abundances, expression patterns, affinities for downstream partners, and turnover rates, we show here from analysis of recombinant Arabidopsis chromoproteins that the Phy isoforms also display distinct biophysical properties. Included are a hypsochromic shift in the Pr absorption for PhyC and varying rates of Pfr to Pr thermal reversion, part of which can be attributed to the core photosensory module in each. Most strikingly, PhyB combines strong temperature dependence of thermal reversion with an order-of-magnitude faster rate to likely serve as the main physiological thermosensor, whereby thermal reversion competes with photoconversion. In addition, comparisons of Pfr occupancies for PhyA and PhyB under a range of red- and white-light fluence rates imply that low-light environments are effectively sensed by PhyA, while high-light environments, such as full sun, are effectively sensed by PhyB. Parallel analyses of the Phy isoforms from potato and maize showed that the unique features within the Arabidopsis family are conserved, thus indicating that the distinct biophysical properties among plant Phy isoforms emerged early in Phy evolution, likely to enable full interrogation of their light and temperature environments.

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34

Mishra, Tanuja, Harcharan S. Dhaliwal, Karan Singh, and Nasib Singh. "Shilajit (Mumie): Current Status of Biochemical, Therapeutic and Clinical Advances." Current Nutrition & Food Science 15, no. 2 (2019): 104–20. http://dx.doi.org/10.2174/1573401313666170823160217.

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Background: Shilajit (mumie), a natural multi-component herbomineral ethnomedicinal food, is used as a traditional medicine for enhancing the quality of life and for management of health ailments in many countries of the world. Use of Shilajit as an adaptogen, aphrodisiac, rejuvenator and anti-aging substance is mentioned in many ancient texts. This review aims to provide comprehensive insights into its biochemical aspects, microbial role in biosynthesis, bioactivities and to establish correlation between traditional uses and scientifically validated research findings. Methods: Scientific literature and ethnopharmacological information were compiled from the published peer-reviewed articles, unpublished materials, thesis, books, patent databases, clinical trial registries and from the websites of research councils of traditional medicine. The scientific databases, thesis repositories and books databases were searched with keywords Shilajit, mumie, mumijo, salajeet, asphaltum, fulvic acid, dibenzo-alpha-pyrones etc. Results: Scientifically validated research and ancient texts suggest multifaceted benefits of Shilajit. It is endowed with anti-stress, memory and energy enhancing, antioxidant, anti-inflammatory, antidiabetic, spermatogenic, neuroprotective, antiulcer and wound healing activities. These pharmacological effects are mainly attributed to the presence of humic acid, fulvic acid, dibenzo-&#945;-pyrones, dibenzo- &#945;-pyrones chromoproteins and trace elements. Conclusion: This review summarizes the traditional importance of Shilajit for the treatment and prevention of several acute and chronic diseases and health ailments. Despite numerous health claims, there are still major gaps in our understanding of its mechanism of action, variability in efficacy and toxicity profile. Therefore, a coordinated interdisciplinary approach is needed to establish the underlying mechanisms of action, comprehensive toxicological profile, pharmacokinetics parameters and effects on different organ systems. Regulatory and governmental impetus to basic and clinical research, safety testing and formulations quality control is warranted.

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35

Borucki, Berthold, Harald Otto, and Maarten P. Heyn. "Reorientation of the Retinylidene Chromophore in the K, L, and M Intermediates of Bacteriorhodopsin from Time-Resolved Linear Dichroism: Resolving Kinetically and Spectrally Overlapping Intermediates of Chromoproteins." Journal of Physical Chemistry B 103, no. 30 (1999): 6371–83. http://dx.doi.org/10.1021/jp990679x.

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36

Sakata, Nobuo, Toshiyuki Mase, Souichi Ikeno, Makoto Hori, Toshio Otani, and Masa Hamada. "DNA Homology Between Chromoprotein Antibiotic Producers." Actinomycetologica 7, no. 1 (1993): 31–36. http://dx.doi.org/10.3209/saj.7_31.

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37

Serlin, Bruce S., and Stanley J. Roux. "Light-induced import of the chromoprotein, phytochrome, into mitochondria." Biochimica et Biophysica Acta (BBA) - Bioenergetics 848, no. 3 (1986): 372–77. http://dx.doi.org/10.1016/0005-2728(86)90213-6.

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38

Schaffner, K., S. E. Braslavsky, and Alfred Holzwarth. "Photophysics and photochemistry of phytochrome, a chromoprotein in plants." Pure and Applied Chemistry 62, no. 7 (1990): 1421–26. http://dx.doi.org/10.1351/pac199062071421.

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39

Pettikiriarachchi, Anne, Lan Gong, Matthew A. Perugini, Rodney J. Devenish, and Mark Prescott. "Ultramarine, a Chromoprotein Acceptor for Förster Resonance Energy Transfer." PLoS ONE 7, no. 7 (2012): e41028. http://dx.doi.org/10.1371/journal.pone.0041028.

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40

Bao, Letian, P. Navaneeth K. Menon, Josefine Liljeruhm, and Anthony C. Forster. "Overcoming chromoprotein limitations by engineering a red fluorescent protein." Analytical Biochemistry 611 (December 2020): 113936. http://dx.doi.org/10.1016/j.ab.2020.113936.

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41

Gildikov, Dmitriy, Stanislav Kumirov, and Ol'ga Petrova. "Study of efficacy of the drug «Hepatojekt»® in complex therapy of hepatitis in dogs." Russian veterinary journal 2020, no. 3 (2020): 28–33. http://dx.doi.org/10.32416/2500-4379-2020-3-28-33.

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The article presents the results of the study of the efficacy of the drug «Hepatojekt»® containing L-ornithine, L-citrulin, L-arginine and auxiliary substances in the treatment of hepatitis initiated by Babesia canis in dogs. The experiment confirmed that the imidocarb-based drug («Piro-stop»®) has antiprotozoal action against the simplest genus Babesia. It has been established that the inclusion of the «Hepatojekt»® drug in the treatment regimen for dogs with hepatitis due to babesiosis, in comparison with basic therapy, contributes to a reliable correction of their carbohydrate and chromoprotein metabolism.

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42

Kunz, Ralf, Kõu Timpmann, June Southall, Richard J. Cogdell, Arvi Freiberg, and Jürgen Köhler. "Fluctuations in the Electron-Phonon Coupling of a Single Chromoprotein." Angewandte Chemie International Edition 52, no. 33 (2013): 8726–30. http://dx.doi.org/10.1002/anie.201303231.

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43

Kunz, Ralf, Kõu Timpmann, June Southall, Richard J. Cogdell, Arvi Freiberg, and Jürgen Köhler. "Fluctuations in the Electron-Phonon Coupling of a Single Chromoprotein." Angewandte Chemie 125, no. 33 (2013): 8888–92. http://dx.doi.org/10.1002/ange.201303231.

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44

Chiang, Cheng-Yi, Cheng-Chung Lee, Shin-Yi Lo, Andrew H. J. Wang, and Huai-Jen Tsai. "Chromophore Deprotonation State Alters the Optical Properties of Blue Chromoprotein." PLOS ONE 10, no. 7 (2015): e0134108. http://dx.doi.org/10.1371/journal.pone.0134108.

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45

Imajo, Seiichi, Masaji Ishiguro, Toshiyuki Tanaka, Masahiro Hirama, and Alexei Teplyakov. "On the conformation of Phe78 of a chromoprotein antibiotic, neocarzinostatin." Bioorganic & Medicinal Chemistry 3, no. 4 (1995): 429–36. http://dx.doi.org/10.1016/0968-0896(95)00032-c.

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46

Zeidler, Mathias, Christina Lang, Janina Hahn, and Jon Hughes. "Real time spectral analysis during phytochrome chromophore and chromoprotein purification." International Journal of Biological Macromolecules 39, no. 1-3 (2006): 100–103. http://dx.doi.org/10.1016/j.ijbiomac.2006.02.028.

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47

Leet, John E., Daniel R. Schroeder, Sandra J. Hofstead, et al. "Kedarcidin, a new chromoprotein antitumor antibiotic: structure elucidation of kedarcidin chromophore." Journal of the American Chemical Society 114, no. 20 (1992): 7946–48. http://dx.doi.org/10.1021/ja00046a071.

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48

Hariharan, Parameswaran, Christopher Gunasekaran Sudhahar, Shan-Ho Chou, and Der-Hang Chin. "Lipid Bilayer-Assisted Release of an Enediyne Antibiotic from Neocarzinostatin Chromoprotein." Biochemistry 49, no. 35 (2010): 7722–32. http://dx.doi.org/10.1021/bi100735v.

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49

Inoue, Masayuki. "Exploring the Chemistry and Biology of Antitumor Enediyne Chromoprotein C-1027." Bulletin of the Chemical Society of Japan 79, no. 4 (2006): 501–10. http://dx.doi.org/10.1246/bcsj.79.501.

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Baker, James R., Derek N. Woolfson, Frederick W. Muskett, Rhys G. Stoneman, Michael D. Urbaniak, and Stephen Caddick. "Protein–Small Molecule Interactions in Neocarzinostatin, the Prototypical Enediyne Chromoprotein Antibiotic." ChemBioChem 8, no. 7 (2007): 704–17. http://dx.doi.org/10.1002/cbic.200600534.

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