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Ugljen-monoksid dehidrogenaza (akceptor)
Ugljen-monoksid dehidrogenaza (akceptor)
Identifikatori
EC broj	1.2.99.2
CAS broj	64972-88-9
Baze podataka
IntEnz	IntEnz pregled
BRENDA	BRENDA pristup
ExPASy	NiceZyme pregled
KEGG	KEGG pristup
MetaCyc	metabolički put
PRIAM	profil
Strukture PBP	RCSB PDB PDBe PDBj PDBsum
PMC
Pretraga
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PubMed	članci
NCBI	proteini

Ugljen-monoksid dehidrogenaza (akceptor) (EC 1.2.99.2, anaerobna ugljen monoksidna dehidrogenaza, ugljen monoksidna oksigenaza, ugljen-monoksidna dehidrogenaza, ugljen-monoksid:(akceptor) oksidoreduktaza) je enzim sa sistematskim imenom karbon-monoksid:akceptor oksidoreduktaza.^[1]^[2]^[3]^[4] Ovaj enzim katalizuje sledeću hemijsku reakciju:

CO +H₂O + A

\rightleftharpoons

CO₂ + AH₂

Ovaj enzim sadrži [Ni3Fe-4S] klaster i [4Fe-4S] klastere. On koristi mnoge elektronske akceptore, uključujući feredoksin, metil viologen, benzil viologen i flavine, a ne koristi piridinske nukleotide. Ovaj enzim formira deo membranskog multienzimskog kompleksa sa EC 1.12.99.6, hidrogenaza (akceptor), koji katalizuje sledeću reakciju:

CO + H2O

\rightleftharpoons

CO2 + H2.

Reference

^ Bonam, D. & Ludden, P.W. (1987). „Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum”. J. Biol. Chem. 262: 2980—2987. PMID 3029096.
^ Diekert, G. & Ritter, M. (1983). „Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum”. FEBS Lett. 151: 41—44. PMID 6687458.
^ Drennan, C.L., Heo, J., Sintchak, M.D., Schreiter, E. and Ludden, P.W. (2001). „Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase”. Proc. Natl. Acad. Sci. USA. 98: 11973—11978. PMID 11593006.
^ Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. and Meyer, O. (2001). „Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster”. Science. 293: 1281—1285. PMID 11509720.

Literatura

Nicholas C. Price; Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third изд.). USA: Oxford University Press. ISBN 019850229X.
Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 изд.). 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 изд.). Wiley Classics Library. ISBN 0471303097.

Spoljašnje veze

Carbon-monoxide+dehydrogenase+(acceptor) на US National Library of Medicine Medical Subject Headings (MeSH)

[1] Bonam, D. & Ludden, P.W. (1987). „Purification and characterization of carbon monoxide dehydrogenase, a nickel, zinc, iron-sulfur protein, from Rhodospirillum rubrum”. J. Biol. Chem. 262: 2980—2987. PMID 3029096.

[2] Diekert, G. & Ritter, M. (1983). „Purification of the nickel protein carbon monoxide dehydrogenase of Clostridium thermoaceticum”. FEBS Lett. 151: 41—44. PMID 6687458.

[3] Drennan, C.L., Heo, J., Sintchak, M.D., Schreiter, E. and Ludden, P.W. (2001). „Life on carbon monoxide: X-ray structure of Rhodospirillum rubrum Ni-Fe-S carbon monoxide dehydrogenase”. Proc. Natl. Acad. Sci. USA. 98: 11973—11978. PMID 11593006.

[4] Dobbek, H., Svetlitchnyi, V., Gremer, L., Huber, R. and Meyer, O. (2001). „Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] cluster”. Science. 293: 1281—1285. PMID 11509720.

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