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Magnetic susceptibility of hydrogenase from Desulfovibrio vulgaris.

descriptionPublicationkeyboard_double_arrow_right Article 11 Oct 1985 English Journal:Journal of biochemistry, volume 97 (issn: 0021-924X, Copyright policy )
Authors: K, Kimura; H, Inokuchi; H, Nanami; T, Yagi;

pmid: 3897216

Magnetic susceptibility of hydrogenase from Desulfovibrio vulgaris.

Abstract

Magnetization and magnetic susceptibility measurements revealed that the hydrogenase [EC 1.12.2.1] from Desulfovibrio vulgaris Miyazaki F has an independent unpaired electron in its iron-sulfur cluster. The paramagnetic center of the Desulfovibrio hydrogenase is, therefore, different from that in the Chromatium hydrogenase which interacts with another paramagnetic center, probably nickel.

Keywords

Iron-Sulfur Proteins, Magnetics, Hydrogenase, Models, Chemical, Temperature, Desulfovibrio

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
2
Average
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