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1qks

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==Overview==
==Overview==
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Cytochrome cd1-nitrite reductase is a bifunctional enzyme that catalyzes, the one-electron reduction of nitrite to nitric oxide and the, four-electron reduction of oxygen to water. The 1.55 A crystal structure, of the dimeric enzyme from Thiosphaera pantotropha is reported here. The, protein was sequenced from the X-ray structure. Each subunit contains a, covalent c heme with two axial His ligands (His-17, His-69) and a unique, noncovalent d1 heme ligated by Tyr-25 and His-200. The d1 heme is the, mononuclear iron center where both oxygen and nitrite reduction take, place. The two types of heme are located in separate domains whose, arrangement suggests a mechanism requiring domain movement during, catalysis.
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Cytochrome cd1-nitrite reductase is a bifunctional enzyme that catalyzes the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of oxygen to water. The 1.55 A crystal structure of the dimeric enzyme from Thiosphaera pantotropha is reported here. The protein was sequenced from the X-ray structure. Each subunit contains a covalent c heme with two axial His ligands (His-17, His-69) and a unique noncovalent d1 heme ligated by Tyr-25 and His-200. The d1 heme is the mononuclear iron center where both oxygen and nitrite reduction take place. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
==About this Structure==
==About this Structure==
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[[Category: periplasmic]]
[[Category: periplasmic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:00:46 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:44 2008''

Revision as of 12:40, 21 February 2008


1qks, resolution 1.28Å

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CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM

Overview

Cytochrome cd1-nitrite reductase is a bifunctional enzyme that catalyzes the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of oxygen to water. The 1.55 A crystal structure of the dimeric enzyme from Thiosphaera pantotropha is reported here. The protein was sequenced from the X-ray structure. Each subunit contains a covalent c heme with two axial His ligands (His-17, His-69) and a unique noncovalent d1 heme ligated by Tyr-25 and His-200. The d1 heme is the mononuclear iron center where both oxygen and nitrite reduction take place. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.

About this Structure

1QKS is a Single protein structure of sequence from Paracoccus denitrificans with , , and as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.

Reference

The anatomy of a bifunctional enzyme: structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1., Fulop V, Moir JW, Ferguson SJ, Hajdu J, Cell. 1995 May 5;81(3):369-77. PMID:7736589

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