1dy7
From Proteopedia
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CYTOCHROME CD1 NITRITE REDUCTASE, CO COMPLEX
Overview
We have investigated dynamic events after flash photolysis of CO from, reduced cytochrome cd(1) nitrite reductase (NiR) from Paracoccus, pantotrophus (formerly Thiosphaera pantotropha). Upon pulsed illumination, of the cytochrome cd(1)-CO complex, at 460 nm, a rapid (<50 ns) absorbance, change, attributed to dissociation of CO, was observed. This was followed, by a biphasic rearrangement with rate constants of 1.7 x 10(4) and 2.5 x, 10(3) s(-1) at pH 8.0. Both parts of the biphasic rearrangement phases, displayed the same kinetic difference spectrum in the region of 400-660, nm. The slower of the two processes was accompanied by proton uptake from, solution (0.5 proton per active site at pH 7.5-8.5). After, photodissociation, the CO ligand recombined at a rate of 12 s(-1) (at 1 mM, CO ... [(full description)]
About this Structure
1DY7 is a [Single protein] structure of sequence from [Paracoccus pantotrophus] with SO4, DHE, CMO, HEC and GOL as [ligands]. Active as [Oxidoreductase], with EC number [1.9.3.2]. Structure known Active Sites: C1B, D1A and D1B. Full crystallographic information is available from [OCA].
Reference
Proton-coupled structural changes upon binding of carbon monoxide to cytochrome cd1: a combined flash photolysis and X-ray crystallography study., Sjogren T, Svensson-Ek M, Hajdu J, Brzezinski P, Biochemistry. 2000 Sep 12;39(36):10967-74. PMID:10998233
Page seeded by OCA on Tue Oct 30 08:34:30 2007
Categories: Paracoccus pantotrophus | Single protein | Brzezinski, P. | Hajdu, J. | Sjogren, T. | Svensson-Ek, M. | CMO | DHE | GOL | HEC | SO4 | Enzyme | Nitrite reductase | Oxidoreductase