Gvožđe:rusticijanin reduktaza
(Preusmjereno sa stranice Fe(II):rusticijanin oksidoreduktaza)
Gvožđe:rusticijanin reduktaza (EC 1.16.9.1, Cyc2) je enzim sa sistematskim imenom Fe(II):rusticijanin oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
Gvožđe:rusticijanin reduktaza | |||||||||
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Identifikatori | |||||||||
EC broj | 1.16.9.1 | ||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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- Fe(II) + rusticijanin Fe(III) + redukovani rusticijanin
Ovaj enzim sadrži c-tip hema. Enzim iz Aciditiobacillus ferooxidans je komponenta elektron transfernog lanca sa Fe(II), koji se sastoji od ovog enzima, bakarnog proteina rusticijanina, citohroma c4, i citohrom c oksidaze (EC 1.9.3.1).
Reference uredi
- ↑ Blake, R.C., 2nd and Shute, E.A. (1994). „Respiratory enzymes of Thiobacillus ferrooxidans. Kinetic properties of an acid-stable iron:rusticyanin oxidoreductase”. Biochemistry 33: 9220-9228. PMID 8049223.
- ↑ Appia-Ayme, C., Bengrine, A., Cavazza, C., Giudici-Orticoni, M.T., Bruschi, M., Chippaux, M. and Bonnefoy, V. (1998). „Characterization and expression of the co-transcribed cyc1 and cyc2 genes encoding the cytochrome c4 (c552) and a high-molecular-mass cytochrome c from Thiobacillus ferrooxidans ATCC 33020”. FEMS Microbiol. Lett. 167: 171-177. PMID 9809418.
- ↑ Yarzabal, A., Brasseur, G., Ratouchniak, J., Lund, K., Lemesle-Meunier, D., DeMoss, J.A. and Bonnefoy, V. (2002). „The high-molecular-weight cytochrome c Cyc2 of Acidithiobacillus ferrooxidans is an outer membrane protein”. J. Bacteriol. 184: 313-317. PMID 11741873.
- ↑ Yarzabal, A., Appia-Ayme, C., Ratouchniak, J. and Bonnefoy, V. (2004). „Regulation of the expression of the Acidithiobacillus ferrooxidans rus operon encoding two cytochromes c, a cytochrome oxidase and rusticyanin”. Microbiology 150: 2113-2123. PMID 15256554.
- ↑ Taha, T.M., Kanao, T., Takeuchi, F. and Sugio, T. (2008). „Reconstitution of iron oxidase from sulfur-grown Acidithiobacillus ferrooxidans”. Appl. Environ. Microbiol. 74: 6808-6810. PMID 18791023.
- ↑ Castelle, C., Guiral, M., Malarte, G., Ledgham, F., Leroy, G., Brugna, M. and Giudici-Orticoni, M.T. (2008). „A new iron-oxidizing/O2-reducing supercomplex spanning both inner and outer membranes, isolated from the extreme acidophile Acidithiobacillus ferrooxidans”. J. Biol. Chem. 283: 25803-25811. PMID 18632666.
- ↑ Quatrini, R., Appia-Ayme, C., Denis, Y., Jedlicki, E., Holmes, D.S. and Bonnefoy, V. (2009). „Extending the models for iron and sulfur oxidation in the extreme acidophile Acidithiobacillus ferrooxidans”. BMC Genomics 10: #394-394. PMID 19703284.
Literatura uredi
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.