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Journal articles on the topic 'Copper. Amine oxidase. Quinone'

Author: Grafiati

Published: 4 June 2021

Last updated: 18 February 2022

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1

Wilmot, C. M. "Oxygen activation in a copper-containing amine oxidase." Biochemical Society Transactions 31, no. 3 (2003): 493–96. http://dx.doi.org/10.1042/bst0310493.

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The process by which molecular oxygen is activated to enable it to function as an electron acceptor in biology is poorly understood. The quinoprotein copper-containing amine oxidase (CuAO) catalyses the conversion of primary amines into aldehydes. As well as copper, the enzyme contains an organic cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ). Following the formation of aldehyde, the enzyme is left as the two-electron reduced aminoquinol form. Reoxidation of the enzyme back to the resting state uses molecular oxygen, which is reduced to H2O2 in the process, with the additional release o

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2

Collison, D., P. F. Knowles, F. E. Mabbs, et al. "Studies on the active site of pig plasma amine oxidase." Biochemical Journal 264, no. 3 (1989): 663–69. http://dx.doi.org/10.1042/bj2640663.

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Amine oxidase from pig plasma (PPAO) has two bound Cu2+ ions and at least one pyrroloquinoline quinone (PQQ) moiety as cofactors. It is shown that recovery of activity by copper-depleted PPAO is linear with respect to added Cu2+ ions. Recovery of e.s.r. and optical spectral characteristics of active-site copper parallel the recovery of catalytic activity. These results are consistent with both Cu2+ ions contributing to catalysis. Further e.s.r. studies indicate that the two copper sites in PPAO, unlike those in amine oxidases from other sources, are chemically distinct. These comparative studi

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3

Cooper, R. A., P. F. Knowles, D. E. Brown, M. A. McGuirl, and D. M. Dooley. "Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12." Biochemical Journal 288, no. 2 (1992): 337–40. http://dx.doi.org/10.1042/bj2880337.

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The cofactors present in a amine oxidase induced in Escherichia coli K-12 by growth on 2-phenylethylamine have been studied by spectroscopic methods. E.s.r. spectroscopy establishes the presence of cupric copper while resonance Raman spectroscopy on the phenylhydrazine derivative of the enzyme provides strong evidence for the oxidized form of 3,4,6-trihydroxyphenylalanine (TOPA) quinone. The amine oxidase should accordingly be classified as EC 1.4.3.6. This is the first report of such an amine oxidase in a Gram-negative bacterium.

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4

Largeron, Martine. "Aerobic catalytic systems inspired by copper amine oxidases." Pure and Applied Chemistry 92, no. 2 (2020): 233–42. http://dx.doi.org/10.1515/pac-2019-0107.

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AbstractThe goal of sustainable development has been accepted as a common policy in current society. In response to this challenge, the development of green processes which utilize environmentally benign oxidants, reduce chemical waste and handling costs, is highly desirable. Given the widespread importance of imines as pivotal synthetic intermediates and essential pharmacophores in numerous biologically active compounds, various catalytic methods allowing the aerobic oxidation of amines to imines have been developed. Recently, noticeable progress has arisen from the discovery of various quino

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5

McGuirl, M. A., D. E. Brown, C. D. McCahon, P. N. Turowski, and D. M. Dooley. "Copper-quinone interactions in amine oxidases." Journal of Inorganic Biochemistry 43, no. 2-3 (1991): 186. http://dx.doi.org/10.1016/0162-0134(91)84178-c.

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6

TANIZAWA, Katsuyuki. "Molecular Mechanism of Topa Quinone Biogenesis in Copper Amine Oxidase." Kagaku To Seibutsu 35, no. 8 (1997): 569–75. http://dx.doi.org/10.1271/kagakutoseibutsu1962.35.569.

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7

Kim, M., T. Okajima, S. Kishishita, et al. "X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (2002): c298. http://dx.doi.org/10.1107/s0108767302096915.

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8

Mura, Anna, Alessandra Padiglia, Rosaria Medda, Francesca Pintus, Alessandro Finazzi Agrò, and Giovanni Floris. "Properties of copper-free pig kidney amine oxidase: Role of topa quinone." FEBS Letters 580, no. 18 (2006): 4317–24. http://dx.doi.org/10.1016/j.febslet.2006.06.089.

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9

Klinman, Judith P. "The multi-functional topa-quinone copper amine oxidases." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1647, no. 1-2 (2003): 131–37. http://dx.doi.org/10.1016/s1570-9639(03)00077-3.

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10

Largeron, Martine. "Aerobic catalytic systems inspired by copper amine oxidases: recent developments and synthetic applications." Organic & Biomolecular Chemistry 15, no. 22 (2017): 4722–30. http://dx.doi.org/10.1039/c7ob00507e.

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Recently, chemists have developed aerobic quinone-based catalytic systems in order to reproduce enzymatic activity and selectivity of copper amine oxidases but also to expand the scope of amine substrates.

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11

Murakawa, Takeshi, Kazuo Kurihara, Mitsuo Shoji, et al. "Neutron crystallography of copper amine oxidase reveals keto/enolate interconversion of the quinone cofactor and unusual proton sharing." Proceedings of the National Academy of Sciences 117, no. 20 (2020): 10818–24. http://dx.doi.org/10.1073/pnas.1922538117.

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Recent advances in neutron crystallographic studies have provided structural bases for quantum behaviors of protons observed in enzymatic reactions. Thus, we resolved the neutron crystal structure of a bacterial copper (Cu) amine oxidase (CAO), which contains a prosthetic Cu ion and a protein-derived redox cofactor, topa quinone (TPQ). We solved hitherto unknown structures of the active site, including a keto/enolate equilibrium of the cofactor with a nonplanar quinone ring, unusual proton sharing between the cofactor and the catalytic base, and metal-induced deprotonation of a histidine resid

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12

Okajima, Toshihide, Sei'ichiro Kishishita, Yen-Chen Chiu, et al. "Reinvestigation of Metal Ion Specificity for Quinone Cofactor Biogenesis in Bacterial Copper Amine Oxidase†,‡." Biochemistry 44, no. 36 (2005): 12041–48. http://dx.doi.org/10.1021/bi051070r.

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13

Longu, Silvia, Anna Mura, Alessandra Padiglia, Rosaria Medda, and Giovanni Floris. "Mechanism-based inactivators of plant copper/quinone containing amine oxidases." Phytochemistry 66, no. 15 (2005): 1751–58. http://dx.doi.org/10.1016/j.phytochem.2005.06.013.

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14

Mura, Anna, Roberto Anedda, Francesca Pintus, et al. "An important lysine residue in copper/quinone-containing amine oxidases." FEBS Journal 274, no. 10 (2007): 2585–95. http://dx.doi.org/10.1111/j.1742-4658.2007.05793.x.

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15

Mure, Minae, Stephen A. Mills, and Judith P. Klinman. "Catalytic Mechanism of the Topa Quinone Containing Copper Amine Oxidases†." Biochemistry 41, no. 30 (2002): 9269–78. http://dx.doi.org/10.1021/bi020246b.

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16

AGOSTINELLI, Enzo, Giovanna DE MATTEIS, Alessandra SINIBALDI, Bruno MONDOVÌ, and Laura MORPURGO. "Reactions of the oxidized organic cofactor in copper-depleted bovine serum amine oxidase." Biochemical Journal 324, no. 2 (1997): 497–501. http://dx.doi.org/10.1042/bj3240497.

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A novel copper-depleted bovine serum amine oxidase (BSAO), in which about half the molecules contained the organic cofactor in the oxidized form, was prepared by adding a reductant in anaerobic conditions to the cyanide-reacted protein. The CuI-semiquinone formed in these conditions reoxidizes after the removal of copper. The inactive derivative was reduced by benzylamine at approx. 1/1000 the rate of BSAO. The pseudo-first-order reaction was preceded by the formation of a protein–benzylamine complex with dissociation constant, Kd, of 4.9±0.5 mM, similar to the Km of BSAO (2.2 mM). Also the re

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17

LIZCANO, José M., Keith F. TIPTON, and Mercedes UNZETA. "Purification and characterization of membrane-bound semicarbazide-sensitive amine oxidase (SSAO) from bovine lung." Biochemical Journal 331, no. 1 (1998): 69–78. http://dx.doi.org/10.1042/bj3310069.

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Semicarbazide-sensitive amine oxidase (SSAO) has been purified from bovine lung microsomes in a form which is catalytically active and stable to storage. The enzyme, an integral membrane protein, was solubilized with Triton X-100 and purification was achieved, in the presence of detergent, by chromatography with Cibacron Blue 3GA-agarose, hydroxylapatite, Lens culinaris-agarose, Resource Q-FPLC and gel filtration on Superdex 200 HR-FPLC. This is the first reported procedure for the extensive purification of a membrane-bound SSAO. The purified enzyme had an apparent Mr of 400000 but exhibited m

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18

Samuels, Nicole M., and Judith P. Klinman. "2,4,5-Trihydroxyphenylalanine Quinone Biogenesis in the Copper Amine Oxidase fromHansenula polymorphawith the Alternate Metal Nickel†." Biochemistry 44, no. 43 (2005): 14308–17. http://dx.doi.org/10.1021/bi051176m.

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19

ANTHONY, Christopher. "Quinoprotein-catalysed reactions." Biochemical Journal 320, no. 3 (1996): 697–711. http://dx.doi.org/10.1042/bj3200697.

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This review is concerned with the structure and function of the quinoprotein enzymes, sometimes called quinoenzymes. These have prosthetic groups containing quinones, the name thus being analogous to the flavoproteins containing flavin prosthetic groups. Pyrrolo-quinoline quinone (PQQ) is non-covalently attached, whereas tryptophan tryptophylquinone (TTQ), topa-quinone (TPQ) and lysine tyrosylquinone (LTQ) are derived from amino acid residues in the backbone of the enzymes. The mechanisms of the quinoproteins are reviewed and related to their recently determined three-dimensional structures. A

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20

Ruggiero, Christy E., and David M. Dooley. "Stoichiometry of the Topa Quinone Biogenesis Reaction in Copper Amine Oxidases†." Biochemistry 38, no. 10 (1999): 2892–98. http://dx.doi.org/10.1021/bi9824994.

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21

Ruggiero, Christy E., and David M. Dooley. "Stoichiometry of the Topa Quinone Biogenesis Reaction in Copper Amine Oxidases." Biochemistry 38, no. 29 (1999): 9556. http://dx.doi.org/10.1021/bi9950802.

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22

Frébort, Ivo, and Osao Adachi. "Copper/quinone-containing amine oxidases, an exciting class of ubiquitous enzymes." Journal of Fermentation and Bioengineering 80, no. 6 (1995): 625–32. http://dx.doi.org/10.1016/0922-338x(96)87746-4.

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23

AGOSTINELLI, Enzo, Giovanna DE MATTEIS, Bruno MONDOVÌ, and Laura MORPURGO. "Reconstitution of Cu2+-depleted bovine serum amine oxidase with Co2+*." Biochemical Journal 330, no. 1 (1998): 383–87. http://dx.doi.org/10.1042/bj3300383.

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Two different Cu2+-depleted derivatives of bovine serum amine oxidase (BSAO) have recently been prepared, which contain about 0.5 mol/dimer of phenylhydrazine-reactive topa quinone (TPQ) cofactor and, depending on the reagents used, about 0.2 or 0.7 residual Cu2+/dimer [Agostinelli, De Matteis, Sinibaldi, Mondovì and Morpurgo (1997) Biochem. J. 324, 497-501]. The benzylamine oxidase activity of both derivatives was < 5% and increased up to ≈ 20% on incorporation of Co2+, irrespective of the residual Cu2+ content, which was unaffected by the treatment according to atomic absorption and ESR s

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24

Turowski, P. N., M. A. McGuirl, and D. M. Dooley. "Intramolecular electron transfer rate between active-site copper and topa quinone in pea seedling amine oxidase." Journal of Biological Chemistry 268, no. 24 (1993): 17680–82. http://dx.doi.org/10.1016/s0021-9258(17)46757-3.

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25

Cai, D., and J. P. Klinman. "Evidence of a self-catalytic mechanism of 2,4,5-trihydroxyphenylalanine quinone biogenesis in yeast copper amine oxidase." Journal of Biological Chemistry 269, no. 51 (1994): 32039–42. http://dx.doi.org/10.1016/s0021-9258(18)31595-3.

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26

Tanizawa, K., and M. Mure. "Coordination of copper in bacterial amine oxidase and its role in the biogenesis of topa quinone cofactor." Journal of Inorganic Biochemistry 67, no. 1-4 (1997): 53. http://dx.doi.org/10.1016/s0162-0134(97)89934-5.

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27

SAYSELL, Colin G., Winston S. TAMBYRAJAH, Jeremy M. MURRAY, et al. "Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue." Biochemical Journal 365, no. 3 (2002): 809–16. http://dx.doi.org/10.1042/bj20011435.

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Copper amine oxidases are homodimeric enzymes containing one Cu2+ ion and one 2,4,5-trihydroxyphenylalanine quinone (TPQ) per monomer. Previous studies with the copper amine oxidase from Escherichia coli (ECAO) have elucidated the structure of the active site and established the importance in catalysis of an active-site base, Asp-383. To explore the early interactions of substrate with enzyme, we have used tranylcypromine (TCP), a fully reversible competitive inhibitor, with wild-type ECAO and with the active-site base variants D383E and D383N. The formation of an adduct, analogous to the subs

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28

MEDDA, Rosaria, Alessandra PADIGLIA, Andrea BELLELLI, et al. "Intermediates in the catalytic cycle of lentil (Lens esculenta) seedling copper-containing amine oxidase1." Biochemical Journal 332, no. 2 (1998): 431–37. http://dx.doi.org/10.1042/bj3320431.

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Spectrophotometry and rapid-scanning stopped-flow spectroscopy have been used to investigate the visible absorbance changes that occur in the course of the reduction of lentil (Lens esculenta) seedling amine oxidase by substrate. The catalytic cycle of the enzyme employs several intermediates but, owing to kinetic limitations, some of them were not identified in previous studies. In this study we have examined several substrates, either rapidly reacting (e.g. putrescine) or slowly reacting (e.g. γ-aminobutanoic acid). Two forms of the enzyme, namely the Cu(I)-aminoresorcinol and quinone ketimi

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29

Williams, Neal K., and Judith P. Klinman. "Whence topa? Models for the biogenesis of topa quinone in copper amine oxidases." Journal of Molecular Catalysis B: Enzymatic 8, no. 1-3 (2000): 95–101. http://dx.doi.org/10.1016/s1381-1177(99)00071-5.

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30

Murakawa, Takeshi, Hideyuki Hayashi, Tomoko Sunami, et al. "High-resolution crystal structure of copper amine oxidase fromArthrobacter globiformis: assignment of bound diatomic molecules as O2." Acta Crystallographica Section D Biological Crystallography 69, no. 12 (2013): 2483–94. http://dx.doi.org/10.1107/s0907444913023196.

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The crystal structure of a copper amine oxidase fromArthrobacter globiformiswas determined at 1.08 Å resolution with the use of low-molecular-weight polyethylene glycol (LMW PEG; average molecular weight ∼200) as a cryoprotectant. The final crystallographicRfactor andRfreewere 13.0 and 15.0%, respectively. Several molecules of LMW PEG were found to occupy cavities in the protein interior, including the active site, which resulted in a marked reduction in the overallBfactor and consequently led to a subatomic resolution structure for a relatively large protein with a monomer molecular weight of

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31

Schwartz, Benjamin, Amy K. Olgin, and Judith P. Klinman. "The Role of Copper in Topa Quinone Biogenesis and Catalysis, as Probed by Azide Inhibition of a Copper Amine Oxidase from Yeast†." Biochemistry 40, no. 9 (2001): 2954–63. http://dx.doi.org/10.1021/bi0021378.

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32

Dainese, Enrico, Annalaura Sabatucci, Francesca Pintus, et al. "Domain mobility as probed by small-angle X-ray scattering may account for substrate access to the active site of two copper-dependent amine oxidases." Acta Crystallographica Section D Biological Crystallography 70, no. 8 (2014): 2101–10. http://dx.doi.org/10.1107/s1399004714012140.

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Amine oxidases are a family of dimeric enzymes that contain one copper(II) ion and one 2,4,5-trihydroxyphenyalanine quinone per subunit. Here, the low-resolution structures of two Cu/TPQ amine oxidases from lentil (Lens esculenta) seedlings and fromEuphorbia characiaslatex have been determined in solution by small-angle X-ray scattering. The active site of these enzymes is highly buried and requires a conformational change to allow substrate access. The study suggests that the funnel-shaped cavity located between the D3 and D4 domains is narrower within the crystal structure, whereas in soluti

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33

Morpurgo, L., O. Befani, S. Sabatini, et al. "Spectroscopic studies of the reaction between bovine serum amine oxidase (copper-containing) and some hydrazides and hydrazines." Biochemical Journal 256, no. 2 (1988): 565–70. http://dx.doi.org/10.1042/bj2560565.

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The carbonyl cofactor of bovine serum amine oxidase, recently identified as pyrroloquinoline quinone [Ameyama, Hayashi, Matsushita, Shinagawa & Adachi (1984) Agric. Biol. Chem. 48, 561-565; Lobenstein-Verbeek, Jongejan, Frank & Duine (1984) FEBS Lett. 170, 305-309], reacts stoichiometrically and irreversibly with hydrazides of phenylacetic acid and of benzoic acid. With the phenylacetic hydrazides a reversible intermediate step was detected by competition with substrate, carbonylic reagents or phenylhydrazine, a typical inhibitor of the enzyme. All hydrazides form an intense broad band

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34

Matsunami, Hideyuki, Toshihide Okajima, Shun Hirota, et al. "Chemical Rescue of a Site-Specific Mutant of Bacterial Copper Amine Oxidase for Generation of the Topa Quinone Cofactor†." Biochemistry 43, no. 8 (2004): 2178–87. http://dx.doi.org/10.1021/bi0361923.

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35

Matsunami, Hideyuki, Toshihide Okajima, Shun Hirota, et al. "Chemical Rescue of a Site-Specific Mutant of Bacterial Copper Amine Oxidase for Generation of the Topa Quinone Cofactor." Biochemistry 43, no. 20 (2004): 6360. http://dx.doi.org/10.1021/bi040021w.

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36

Didier, Amandine, David Ricard, Maurice L'Her, and Bernard Boitrel. "Tripodal and/or picket porphyrins to mimic the cytochrome c oxidase activity." Journal of Porphyrins and Phthalocyanines 07, no. 04 (2003): 282–90. http://dx.doi.org/10.1142/s1088424603000379.

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The efficiency of different series of tris-(2-aminoethyl)amine TREN-capped porphyrins as catalysts for the electroreduction of dioxygen has been studied after adsorption of the molecules at the surface of a graphite electrode. The influence of two structural features have been explored: the relative position of the two metals in the iron-copper bimetallic complexes and the nature of the benzyl groups of the tripod itself. These compounds have also been compared with picket porphyrins bearing aromatic amino functions, e.g. quinoline. The conclusions obtained in the case of TREN-capped catalysts

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37

Hirota, Shun, Takahiro Iwamoto, Katsuyuki Tanizawa, Osao Adachi, and Osamu Yamauchi. "Spectroscopic Characterization of Carbon Monoxide Complexes Generated for Copper/Topa Quinone-Containing Amine Oxidases†." Biochemistry 38, no. 43 (1999): 14256–63. http://dx.doi.org/10.1021/bi991129s.

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38

Mu, D., S. M. Janes, A. J. Smith, D. E. Brown, D. M. Dooley, and J. P. Klinman. "Tyrosine codon corresponds to topa quinone at the active site of copper amine oxidases." Journal of Biological Chemistry 267, no. 12 (1992): 7979–82. http://dx.doi.org/10.1016/s0021-9258(18)42395-2.

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39

DuBois, Jennifer L., and Judith P. Klinman. "The Nature of O2Reactivity Leading to Topa Quinone in the Copper Amine Oxidase fromHansenula polymorphaand Its Relationship to Catalytic Turnover†." Biochemistry 44, no. 34 (2005): 11381–88. http://dx.doi.org/10.1021/bi0504759.

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40

Lee, Younghee, and Lawrence M. Sayre. "Model studies on the quinone-containing copper amine oxidases. Unambiguous demonstration of a transamination mechanism." Journal of the American Chemical Society 117, no. 48 (1995): 11823–28. http://dx.doi.org/10.1021/ja00153a001.

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41

Agostinelli, Enzo, Francesca Belli, Laura Dalla Vedova, Silvia Longu, Anna Mura, and Giovanni Floris. "Catalytic Properties and the Role of Copper in Bovine and Lentil Seedling Copper/Quinone-Containing Amine Oxidases: Controversial Opinions." European Journal of Inorganic Chemistry 2005, no. 9 (2005): 1635–41. http://dx.doi.org/10.1002/ejic.200401020.

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42

Šebela, Marek, Lenka Luhová, Ivo Frébort, et al. "Analysis of the active sites of copper/topa quinone-containing amine oxidases fromLathyrus odoratus andL. sativus seedlings." Phytochemical Analysis 9, no. 5 (1998): 211–22. http://dx.doi.org/10.1002/(sici)1099-1565(199809/10)9:5<211::aid-pca407>3.0.co;2-x.

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43

DuBois, Jennifer L., and Judith P. Klinman. "Mechanism of post-translational quinone formation in copper amine oxidases and its relationship to the catalytic turnover." Archives of Biochemistry and Biophysics 433, no. 1 (2005): 255–65. http://dx.doi.org/10.1016/j.abb.2004.08.036.

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44

MÄKI, Joni M., and Kari I. KIVIRIKKO. "Cloning and characterization of a fourth human lysyl oxidase isoenzyme." Biochemical Journal 355, no. 2 (2001): 381–87. http://dx.doi.org/10.1042/bj3550381.

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We report here the complete cDNA sequence and exon-intron organization of the human lysyl oxidase-like (LOXL)3 gene, a new member of the lysyl oxidase (LO) gene family. The predicted polypeptide is 753 amino acids in length, including a signal peptide of 25 residues. The C-terminal region, residues 529-729, contains a LO domain similar to those in the LOX (the first characterized LO isoenzyme), LOXL and LOXL2 polypeptides. It possesses the putative copper binding sequence, and the lysine and tyrosine residues that form the lysyltyrosyl quinone cofactor. The N-terminal region, which is similar

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45

Frébort, Ivo, Kazunobu Matsushita, and Osao Adachi. "Involvement of multiple copper/topa quinone-containing and flavin-containing amine oxidases and NAD(P)+ aldehyde dehydrogenases in amine degradation by filamentous fungi." Journal of Fermentation and Bioengineering 84, no. 3 (1997): 200–212. http://dx.doi.org/10.1016/s0922-338x(97)82055-7.

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46

Shepard, Eric M., Gregory A. Juda, Ke-Qing Ling, Lawrence M. Sayre, and David M. Dooley. "Cyanide as a copper and quinone-directed inhibitor of amine oxidases from pea seedlings (Pisum sativum) and Arthrobacter globiformis: evidence for both copper coordination and cyanohydrin derivatization of the quinone cofactor." JBIC Journal of Biological Inorganic Chemistry 9, no. 4 (2004): 507. http://dx.doi.org/10.1007/s00775-004-0557-9.

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47

Shepard, Eric M., Gregory A. Juda, Ke-Qing Ling, Lawrence M. Sayre, and David M. Dooley. "Cyanide as a copper and quinone-directed inhibitor of amine oxidases from pea seedlings (Pisum sativum) and Arthrobacter globiformis: evidence for both copper coordination and cyanohydrin derivatization of the quinone cofactor." JBIC Journal of Biological Inorganic Chemistry 9, no. 3 (2004): 256–68. http://dx.doi.org/10.1007/s00775-004-0522-7.

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48

Lee, Younghee, and Lawrence M. Sayre. "Model Reactions for the Quinone-Containing Copper Amine Oxidases. Anaerobic Reaction Pathways and Catalytic Aerobic Deamination of Activated Amines in Buffered Aqueous Acetonitrile." Journal of the American Chemical Society 117, no. 11 (1995): 3096–105. http://dx.doi.org/10.1021/ja00116a014.

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49

Mandal, Subrata, Younghee Lee, Matthew M. Purdy, and Lawrence M. Sayre. "Chemical Simulation of Biogenesis of the 2,4,5-Trihydroxyphenylalanine Quinone Cofactor of Copper Amine Oxidases: Mechanistic Distinctions Point toward a Unique Role of the Active Site in theo-Quinone Water Addition Step†." Journal of the American Chemical Society 122, no. 15 (2000): 3574–84. http://dx.doi.org/10.1021/ja992886g.

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50

Xu, Jingjing, Ziqiao Ding, Bing Liu, et al. "Structure of the cytochrome aa3-600 heme-copper menaquinol oxidase bound to inhibitor HQNO shows TM0 is part of the quinol binding site." Proceedings of the National Academy of Sciences 117, no. 2 (2019): 872–76. http://dx.doi.org/10.1073/pnas.1915013117.

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Abstract:

Virtually all proton-pumping terminal respiratory oxygen reductases are members of the heme-copper oxidoreductase superfamily. Most of these enzymes use reduced cytochrome c as a source of electrons, but a group of enzymes have evolved to directly oxidize membrane-bound quinols, usually menaquinol or ubiquinol. All of the quinol oxidases have an additional transmembrane helix (TM0) in subunit I that is not present in the related cytochrome c oxidases. The current work reports the 3.6-Å-resolution X-ray structure of the cytochrome aa3-600 menaquinol oxidase from Bacillus subtilis containing 1 e

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