Literature DB >> 11456747

Theoretical modeling of putative Ni(III)--F(430) intermediates of methylcoenzyme M reductase.

T Wondimagegn1, A Ghosh.   

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Year:  2001        PMID： 11456747     DOI： 10.1021/ja001870j

Source DB:  PubMed          Journal:  J Am Chem Soc        ISSN： 0002-7863            Impact factor:   15.419


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  4 in total

1.  Transition metal spin state energetics and noninnocent systems: challenges for DFT in the bioinorganic arena.

Authors:  Abhik Ghosh
Journal:  J Biol Inorg Chem       Date:  2006-07-14       Impact factor: 3.358

2.  Spectroscopic and computational characterization of the nickel-containing F430 cofactor of methyl-coenzyme M reductase.

Authors:  Jennifer L Craft; Yih-Chern Horng; Stephen W Ragsdale; Thomas C Brunold
Journal:  J Biol Inorg Chem       Date:  2003-12-09       Impact factor: 3.358

3.  Probing the reactivity of Ni in the active site of methyl-coenzyme M reductase with substrate analogues.

Authors:  Meike Goenrich; Felix Mahlert; Evert C Duin; Carsten Bauer; Bernhard Jaun; Rudolf K Thauer
Journal:  J Biol Inorg Chem       Date:  2004-06-15       Impact factor: 3.358

4.  Coordination and binding geometry of methyl-coenzyme M in the red1m state of methyl-coenzyme M reductase.

Authors:  Dariush Hinderberger; Sieglinde Ebner; Stefan Mayr; Bernhard Jaun; Markus Reiher; Meike Goenrich; Rudolf K Thauer; Jeffrey Harmer
Journal:  J Biol Inorg Chem       Date:  2008-08-19       Impact factor: 3.358
  4 in total

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