Search Results - "Rajagopalan, K V"
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1
Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
Published in Nature (London) (15-11-2001)“…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…”
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2
Layer-by-Layer Arrangement by Protein−Protein Interaction of Sulfite Oxidase and Cytochrome c Catalyzing Oxidation of Sulfite
Published in Journal of the American Chemical Society (30-01-2008)“…Layer-by-layer self-assembly of sulfite oxidase and cytochrome c was carried out without additional polymeric polyelectrolytes. The arrangement shows a linear…”
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Effect of Exchange of the Cysteine Molybdenum Ligand with Selenocysteine on the Structure and Function of the Active Site in Human Sulfite Oxidase
Published in Biochemistry (Easton) (19-11-2013)“…Sulfite oxidase (SO) is an essential molybdoenzyme for humans, catalyzing the final step in the degradation of sulfur-containing amino acids and lipids, which…”
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4
Structure-Based Alteration of Substrate Specificity and Catalytic Activity of Sulfite Oxidase from Sulfite Oxidation to Nitrate Reduction
Published in Biochemistry (Easton) (14-02-2012)“…Eukaryotic sulfite oxidase is a dimeric protein that contains the molybdenum cofactor and catalyzes the metabolically essential conversion of sulfite to…”
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5
Structure of the Molybdenum Site of Escherichia coli Trimethylamine N-Oxide Reductase
Published in Inorganic chemistry (04-02-2008)“…We report a structural characterization of the molybdenum site of recombinant Escherichia coli trimethylamine N-oxide (TMAO) reductase using X-ray absorption…”
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6
Evidence for the Physiological Role of a Rhodanese-Like Protein for the Biosynthesis of the Molybdenum Cofactor in Humans
Published in Proceedings of the National Academy of Sciences - PNAS (20-04-2004)“…Recent studies have identified the human genes involved in the biosynthesis of the molybdenum cofactor. The human MOCS3 protein contains an N-terminal domain…”
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7
Crystal Structure of DMSO Reductase: Redox-Linked Changes in Molybdopterin Coordination
Published in Science (American Association for the Advancement of Science) (14-06-1996)“…The molybdoenzyme dimethylsulfoxide (DMSO) reductase contributes to the release of dimethylsulfide, a compound that has been implicated in cloud nucleation and…”
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Crystal Structure of a Molybdopterin Synthase−Precursor Z Complex: Insight into Its Sulfur Transfer Mechanism and Its Role in Molybdenum Cofactor Deficiency
Published in Biochemistry (Easton) (15-01-2008)“…In almost all biological life forms, molybdenum and tungsten are coordinated by molybdopterin (MPT), a tricyclic pyranopterin containing a cis-dithiolene…”
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9
In Vitro Molybdenum Ligation to Molybdopterin Using Purified Components
Published in The Journal of biological chemistry (04-03-2005)“…We have previously shown that Escherichia coli MoeA and MogA are required in vivo for the final step of molybdenum cofactor biosynthesis, the addition of the…”
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Structural Insights into Sulfite Oxidase Deficiency
Published in The Journal of biological chemistry (30-09-2005)“…Sulfite oxidase deficiency is a lethal genetic disease that results from defects either in the genes encoding proteins involved in molybdenum cofactor…”
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11
The Structures of the C185S and C185A Mutants of Sulfite Oxidase Reveal Rearrangement of the Active Site
Published in Biochemistry (Easton) (11-05-2010)“…Sulfite oxidase (SO) catalyzes the physiologically critical conversion of sulfite to sulfate. Enzymatic activity is dependent on the presence of the metal…”
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12
Mechanistic and Mutational Studies of Escherichia coli Molybdopterin Synthase Clarify the Final Step of Molybdopterin Biosynthesis
Published in The Journal of biological chemistry (18-04-2003)“…Biosynthesis of the molybdenum cofactor, a chelate of molybdenum or tungsten with a novel pterin, occurs in virtually all organisms including humans. In the…”
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A Sulfurtransferase Is Required in the Transfer of Cysteine Sulfur in the in Vitro Synthesis of Molybdopterin from Precursor Z in Escherichia coli
Published in The Journal of biological chemistry (22-06-2001)“…It has been shown that conversion of precursor Z to molybdopterin (MPT) by Escherichia coli MPT synthase entails the transfer of the sulfur atom of the…”
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14
The Role of Tyrosine 343 in Substrate Binding and Catalysis by Human Sulfite Oxidase
Published in The Journal of biological chemistry (09-04-2004)“…In the crystal structure of chicken sulfite oxidase, the residue Tyr322 (Tyr343 in human sulfite oxidase) was found to directly interact with a bound sulfate…”
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15
Characterization of Escherichia coli MoeB and Its Involvement in the Activation of Molybdopterin Synthase for the Biosynthesis of the Molybdenum Cofactor
Published in The Journal of biological chemistry (14-09-2001)“…Amino acid sequence comparisons ofEscherichia coli MoeB suggested that the MoeB-dependent formation of a C-terminal thiocarboxylate on the MoaD subunit of…”
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16
Structure of the Molybdenum Site of Dimethyl Sulfoxide Reductase
Published in Journal of the American Chemical Society (17-02-1999)“…Molybdenum K-edge X-ray absorption and Mo(V) electron paramagentic resonance (EPR) spectroscopies have been used to probe the metal coordination in oxidized…”
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17
Role of the C-Terminal Gly-Gly Motif of Escherichia Coli MoaD, a Molybdenum Cofactor Biosynthesis Protein with a Ubiquitin Fold
Published in Biochemistry (Easton) (23-01-2007)“…In Escherichia coli, the MoaD protein plays a central role in the conversion of precursor Z to molybdopterin (MPT) during molybdenum cofactor biosynthesis…”
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18
Nature of Halide Binding to the Molybdenum Site of Sulfite Oxidase
Published in Inorganic chemistry (03-10-2011)“…Valuable information on the active sites of molybdenum enzymes has been provided from both MoV electron paramagnetic resonance (EPR) spectroscopy and X-ray…”
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Modified Active Site Coordination in a Clinical Mutant of Sulfite Oxidase
Published in Journal of the American Chemical Society (01-08-2007)“…The molybdenum site of the Arginine 160 → Glutamine clinical mutant of the physiologically vital enzyme sulfite oxidase has been investigated by a combination…”
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High-Resolution EXAFS of the Active Site of Human Sulfite Oxidase: Comparison with Density Functional Theory and X-ray Crystallographic Results
Published in Inorganic chemistry (23-01-2006)“…Much of our knowledge about molybdenum enzymes has originated from EXAFS spectroscopy. This technique provides excellent bond-length accuracy but has only…”
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