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1qks
From Proteopedia
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[[Image:1qks.jpg|left|200px]] | [[Image:1qks.jpg|left|200px]] | ||
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'''CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM''' | '''CYTOCHROME CD1 NITRITE REDUCTASE, OXIDISED FORM''' | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fulop, V.]] | [[Category: Fulop, V.]] | ||
| - | [[Category: | + | [[Category: Denitrification]] |
| - | [[Category: | + | [[Category: Electron transport]] |
| - | [[Category: | + | [[Category: Enzyme]] |
| - | [[Category: | + | [[Category: Nitrite reductase]] |
| - | [[Category: | + | [[Category: Oxidoreductase]] |
| - | [[Category: | + | [[Category: Periplasmic]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:23:45 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:23, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 06:23:45 2008
