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Proximal histidine redox potential

The [4Fe-4S] clusters in D. gigas hydrogenase, unusually, show pH-dependent redox potentials, which means that they transfer protons and electrons at the same time. The distal cluster has a histidine ligand near the surface and so it presumably acquires a proton from the solution on reduction. The proximal cluster is distant from the surface, but there is a potential channel for protons leading to the [NiFe]-center, where protons are involved in the cataljdic reaction. Thus when the [NiFe]-center reduces the proximal cluster, both an electron and a proton can be transferred, at least as far as the [3Fe-4S] cluster. [Pg.1158]


See other pages where Proximal histidine redox potential is mentioned: [Pg.110]    [Pg.88]    [Pg.123]    [Pg.181]    [Pg.349]    [Pg.47]    [Pg.70]    [Pg.71]    [Pg.1897]    [Pg.2314]    [Pg.796]    [Pg.1896]    [Pg.2313]    [Pg.359]    [Pg.267]    [Pg.90]    [Pg.318]    [Pg.1395]    [Pg.473]    [Pg.319]   
See also in sourсe #XX -- [ Pg.70 ]




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Proximal

Proximal histidine

Proximates

Proximation

Proximity

Redox potentials

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