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molybdopterin guanine dinucleotide

National Institutes of Health

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2 relations

Broader (2)

Guanine NucleotidesPterins

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2000
Highly Cited
2000
Mechanism of Assembly of the Bis(Molybdopterin Guanine Dinucleotide)Molybdenum Cofactor in Rhodobacter sphaeroidesDimethyl Sulfoxide Reductase*
A fully defined in vitro system has been developed for studying the mechanism of assembly of the bis(molybdopterin guanine… Expand
Highly Cited
2000
Highly Cited
2000
The Crystal Structure of the Escherichia coliMobA Protein Provides Insight into Molybdopterin Guanine Dinucleotide Biosynthesis*
The molybdenum cofactor (Moco) is found in a variety of enzymes present in all phyla and comprises a family of related molecules… Expand
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Highly Cited
1999
Highly Cited
1999
The genetic basis of tetrathionate respiration in Salmonella typhimurium
A range of bacteria are able to use tetrathionate as a terminal respiratory electron acceptor. Here we report the identification… Expand
Highly Cited
1998
Highly Cited
1998
Selenium-containing formate dehydrogenase H from Escherichia coli: a molybdopterin enzyme that catalyzes formate oxidation without oxygen transfer.
Formate dehydrogenase H, FDH(Se), from Escherichia coli contains a molybdopterin guanine dinucleotide cofactor and a… Expand
Highly Cited
1997
Highly Cited
1997
Crystal Structure of Formate Dehydrogenase H: Catalysis Involving Mo, Molybdopterin, Selenocysteine, and an Fe4S4 Cluster
Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide… Expand
Highly Cited
1996
Highly Cited
1996
Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination
The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been… Expand
1995
1995
Association of molybdopterin guanine dinucleotide with Escherichia coli dimethyl sulfoxide reductase: effect of tungstate and a mob mutation
We have identified the organic component of the molybdenum cofactor in Escherichia coli dimethyl sulfoxide reductase (DmsABC) to… Expand
Highly Cited
1991
Highly Cited
1991
Molybdopterin adenine dinucleotide and molybdopterin hypoxanthine dinucleotide in formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum (Marburg)
Formylmethanofuran dehydrogenase from Methanobacterium thermoautotrophicum was purified to apparent homogeneity and found to… Expand
Highly Cited
1991
Highly Cited
1991
Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide.
The chlorate-resistant mutants of Escherichia coli are affected in the biosynthesis of the molybdenum cofactor and show… Expand
Highly Cited
1990
Highly Cited
1990
Molybdopterin guanine dinucleotide: a modified form of molybdopterin identified in the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides forma specialis denitrificans.
The nature of molybdenum cofactor in the bacterial enzyme dimethyl sulfoxide reductase has been investigated by application of… Expand
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