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Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB–MoaD complex
The activation of ubiquitin and related protein modifiers is catalysed by members of the E1 enzyme family that use ATP for the covalent self-attachment of the modifiers to a conserved cysteine. The… Expand
Molecular Basis of Sulfite Oxidase Deficiency from the Structure of Sulfite Oxidase
The molybdenum-containing enzyme sulfite oxidase catalyzes the conversion of sulfite to sulfate, the terminal step in the oxidative degradation of cysteine and methionine. Deficiency of this enzyme… Expand
The pterin molybdenum cofactors.
crassa, demonstrated that the inactive apoprotein of nitrate reductase in extracts of the mutant could be reconstituted by the addition of denatured preparations of purified molybdoenzymes from… Expand
The crystal structure of Escherichia coli MoeA and its relationship to the multifunctional protein gephyrin.
BACKGROUND Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in archaea, eubacteria, and eukaryotes. In humans, genetic abnormalities in the biosynthetic pathway… Expand
The role of superoxide anion generation in phagocytic bactericidal activity. Studies with normal and chronic granulomatous disease leukocytes.
- R. Johnston, B. B. Keele, +4 authors K. Rajagopalan
- Medicine, Chemistry
- The Journal of clinical investigation
- 1 June 1975
The capacity of human phagocytes to generate superoxide anion (O2-), a free radical of oxygen, and a possible role for this radical or its derivatives in the killing of phagocytized bacteria were… Expand
The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (type D) to an O2-dependent form (type O).
Abstract Rat liver xanthine dehydrogenase, type D, has been isolated directly from crude extracts as an antibody complex and its properties compared with those of two oxidase forms of the enzyme,… Expand
Identification of the second chromophore of Escherichia coli and yeast DNA photolyases as 5,10-methenyltetrahydrofolate.
- J. L. Johnson, S. Hamm-Alvarez, G. Payne, G. Sancar, K. Rajagopalan, A. Sancar
- Chemistry, Medicine
- Proceedings of the National Academy of Sciences…
- 1 April 1988
Denaturation of DNA photolyase (deoxyribodipyrimidine photolyase, EC 22.214.171.124) from Escherichia coli with guanidine hydrochloride or acidification to pH 2 released, in addition to FAD, a chromophore… Expand
Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
- M. J. Rudolph, M. Wuebbens, K. Rajagopalan, H. Schindelin
- Biology, Medicine
- Nature Structural Biology
Molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes, including humans. Genetic deficiencies of enzymes involved in Moco… Expand
Recombinant Rhodobacter capsulatus Xanthine Dehydrogenase, a Useful Model System for the Characterization of Protein Variants Leading to Xanthinuria I in Humans*
- S. Leimkühler, R. Hodson, G. George, K. Rajagopalan
- Chemistry, Medicine
- Journal of Biological Chemistry
- 6 June 2003
Rhodobacter capsulatus xanthine dehydrogenase (XDH) forms an (αβ)2 heterotetramer and is highly homologous to homodimeric eukaryotic XDHs. The crystal structures of bovine XDH and R. capsulatus XDH… Expand
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 implicated in cloud nucleation and global climate regulation. The crystal… Expand