Multiple four-coordinate forms in a nickel hydrocorphinate related to cofactor F430 of methylreductase

1989 ◽  
Vol 93 (17) ◽  
pp. 6283-6290 ◽  
Author(s):  
John A. Shelnutt
Keyword(s):  
Cofactor F430

Cofactor F430 as a biomarker for methanogenic activity: application to an anaerobic bioreactor system

2017 ◽  
Vol 102 (3) ◽  
pp. 1191-1201 ◽  
Author(s):  
I. Passaris ◽  
P. Van Gaelen ◽  
R. Cornelissen ◽  
K. Simoens ◽  
D. Grauwels ◽  
...  
Keyword(s):  
Anaerobic Bioreactor ◽  
Methanogenic Activity ◽  
Bioreactor System ◽  
Cofactor F430

Electrochemistry of heat-extracted methanogenic bacterial cofactor F430

1990 ◽  
Vol 170 (2) ◽  
pp. 161-163 ◽  
Author(s):  
A.L. Crumbliss ◽  
K.L. McLachlan ◽  
J.N. Siedow ◽  
S.P. Walton
Keyword(s):  
Cofactor F430

scholarly journals A Nickel(II)-Containing Vitamin B12 Derivative with a Cofactor-F430-type π-System

2018 ◽  
Vol 57 (50) ◽  
pp. 16308-16312 ◽  
Author(s):  
Christopher Brenig ◽  
Lucas Prieto ◽  
René Oetterli ◽  
Felix Zelder
Keyword(s):  
Vitamin B12 ◽  
Cofactor F430

Metal Complexes with Macrocyclic Ligands. Part XLII. Tetraazamacrocyclic nickel(II) complexes with a methylthio or a methoxy pendant chain as model for cofactor F430

1996 ◽  
Vol 79 (4) ◽  
pp. 1011-1020 ◽  
Author(s):  
Claudio L. Schmid ◽  
Christian Kempf ◽  
Andreas Taubert ◽  
Markus Neuburger ◽  
Margareta Zehnder ◽  
...  
Keyword(s):  
Metal Complexes ◽  
Macrocyclic Ligands ◽  
Cofactor F430

scholarly journals The magnetic properties of the nickel cofactor F430 in the enzyme methyl-coenzyme M reductase of Methanobacterium thermoautotrophicum

1989 ◽  
Vol 260 (2) ◽  
pp. 613-616 ◽  
Author(s):  
M R Cheesman ◽  
D Ankel-Fuchs ◽  
R K Thauer ◽  
A J Thompson
Keyword(s):  
Magnetic Circular Dichroism ◽  
Methanobacterium Thermoautotrophicum ◽  
Zero Field ◽  
Zero Field Splitting ◽  
Coenzyme M ◽  
Equal Zero ◽  
Magnetic Circular Dichroism Spectroscopy ◽  
Oxygen Ligand ◽  
Methyl Coenzyme M Reductase ◽  
Cofactor F430

Cofactor 430 of methyl-coenzyme M reductase from Methanobacterium thermoautotrophicum was studied in both the extracted form in aqueous solution and protein-bound by using low-temperature magnetic-circular-dichroism spectroscopy. In both forms the nickel was present as high-spin paramagnetic nickel(II), spin S = 1, subject to almost equal zero-field splitting (cofactor F430, D = +9.0 cm-1, E/D = 0; methyl-coenzyme M reductase, D = +8.5 cm-1, [E/D[ = 0.2). This suggests identical axial co-ordination by oxygen ligand(s) both in aqueous cofactor F430 and in the investigated state of the protein.

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