1WUI

Ultra-High resolution Structure Of The Ni-A State Of [Nife]Hydrogenase From Desulufovibrio Vulgaris Miyazaki F

Summary for 1WUI

• Entry DOI: 10.2210/pdb1wui/pdb
• Related: 1WUH 1WUJ 1WUK 1WUL
• Descriptor: Periplasmic [NiFe] hydrogenase small subunit, Periplasmic [NiFe] hydrogenase large subunit, IRON/SULFUR CLUSTER, ... (9 entities in total)
• Functional Keywords: high resolution crystal structure, [nife]hydrogenase, oxidoreductase, ni-a state, unready state
• Biological source: Desulfovibrio vulgaris str. 'Miyazaki F'; More
• Total number of polymer chains: 2
• Total formula weight: 89756.81

Authors

Ogata, H.,Hirota, S.,Nakahara, A.,Komori, H.,Shibata, N.,Kato, T.,Kano, K.,Higuchi, Y. (deposition date: 2004-12-07, release date: 2005-12-07, Last modification date: 2024-10-16)

Primary citation

Ogata, H.,Hirota, S.,Nakahara, A.,Komori, H.,Shibata, N.,Kato, T.,Kano, K.,Higuchi, Y.
Activation process of [NiFe] hydrogenase elucidated by high-resolution X-Ray analyses: conversion of the ready to the unready state
Structure, 13:1635-1642, 2005

PubMed Abstract: Hydrogenases catalyze oxidoreduction of molecular hydrogen and have potential applications for utilizing dihydrogen as an energy source. [NiFe] hydrogenase has two different oxidized states, Ni-A (unready, exhibits a lag phase in reductive activation) and Ni-B (ready). We have succeeded in converting Ni-B to Ni-A with the use of Na2S and O2 and determining the high-resolution crystal structures of both states. Ni-B possesses a monatomic nonprotein bridging ligand at the Ni-Fe active site, whereas Ni-A has a diatomic species. The terminal atom of the bridging species of Ni-A occupies a similar position as C of the exogenous CO in the CO complex (inhibited state). The common features of the enzyme structures at the unready (Ni-A) and inhibited (CO complex) states are proposed. These findings provide useful information on the design of new systems of biomimetic dihydrogen production and fuel cell devices.

PubMed: 16271886
DOI: 10.1016/j.str.2005.07.018

Experimental method

X-RAY DIFFRACTION (1.04 Å)