H2‐forming N5,N10‐methylenetetrahydromethanopterin dehydrogenase: mechanism of H2 formation analyzed using hydrogen isotopes

Klein, Andreas R.; Fernández, Vı́ctor M.; Thauer, Rudolf K.

doi:10.1016/0014-5793(95)00642-m

Cited by 32 publications

(24 citation statements)

References 13 publications

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“…In the presence of CHtH 4 MPT + the enzyme was found to catalyze an H 2 /D + and an H 2 /2D + exchange (reactions 9 and 10) ( Figure 8A) 26,27 and the conversion of ortho and para H 2 (reaction 11) ( Figure 8B). 28 Note that catalysis of these reactions by the metalfree hydrogenase was strictly CHtH 4 MPT + dependent.…”

Section: Catalytic Properties Of the Enzymementioning

confidence: 96%

Reactions with Molecular Hydrogen in Microorganisms: Evidence for a Purely Organic Hydrogenation Catalyst

1996

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Section: Catalytic Properties Of the Enzymementioning

confidence: 96%

Reactions with Molecular Hydrogen in Microorganisms: Evidence for a Purely Organic Hydrogenation Catalyst

1996

Self Cite

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“…There are two kinds of ''true" hydrogen-metabolizing enzymes: the [NiFe]-and [FeFe]-hydrogenases [3]. A third kind, the [FeS] cluster-free-or [Fe]-hydrogenase, is only found in methanogens where it transfers a hydride to methenyltetrahydromethanopterin [4]. X-ray crystallography and FTIR spectroscopy have shown that the three enzymes are characterized by complex active sites that have in common a Fe(CO) x unit, and, in the case of [NiFe]-and [FeFe]-hydrogenases, two CN À ligands ( Fig.…”

Section: Introductionmentioning

confidence: 99%

The role of the maturase HydG in [FeFe]‐hydrogenase active site synthesis and assembly

et al. 2009

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a b s t r a c t[FeFe]-hydrogenases catalyze the protons/hydrogen interconversion through a unique di-iron active site consisting of three CO and two CN ligands, and a non-protein SCH 2 XCH 2 S (X = N or O) dithiolate bridge. Site assembly requires two ''Radical-S-adenosylmethionine (SAM or AdoMet)" iron-sulfur enzymes, HydE and HydG, and one GTPase, HydF. The sequence homology between HydG and ThiH, a Radical-SAM enzyme which cleaves tyrosine into p-cresol and dehydroglycine, and the finding of a similar cleavage reaction catalyzed by HydG suggests a mechanism for hydrogenase maturation. Here we propose that HydG is specifically involved in the synthesis of the dithiolate ligand, with two tyrosine-derived dehydroglycines as precursors along with an [FeS] cluster of HydG functioning both as electron shuttle and source of the sulfur atoms.

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“…This technique was used to study the mechanisms of testosterone metabolism [49] and chemical hydrolysis of penicillinoic acid [50], among many other examples. The H-D exchange was used to study antigen-antibody reactions [34] and mechanisms of H 2 formation by methanogenic bacteria [37]. The use of D labels in many spectroscopic studies [51] illustrates the important contributions of this isotope in current biological research.…”

Section: Solvent and Isotope Effects Of Deuteriummentioning

confidence: 99%

“…Since C-D bonds are much stronger than C-H bonds, the relative reactivity of deuterated compounds can help determine to what extent C-H bond breakage is normally involved. Other aspects of these 'deuterium isotope effects' have been discussed in great detail [35][36][37][38]. Deuterated compounds are extensively used in spectrophotometric studies.…”

Section: Biochemical and Structural Studies On Deuteriummentioning

confidence: 99%

Role of heavy water in biological sciences with an emphasis on thermostabilization of vaccines

Balamurugan¹,

Rajak²,

Chakravarti³

et al. 2009

Expert Review of Vaccines

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Preservation of vaccines, viruses and other biologicals is one of the onerous tasks in maintaining the quality of the products from manufacture until they reach the end users. Live-attenuated viral vaccines, serum immunoglobulins, plasma fractions and clinical samples, including tissues and body fluids, are all materials that usually require cold-chain maintenance during storage and distribution. A number of stabilizers are currently used to help retain the quality of these materials, in particular vaccines, during transit. Deuterium oxide (heavy water; D(2)O) has previously been reported to have a protective effect on biomolecules (proteins and nucleic acids), cells and simple multicellular organisms against thermal shock. Of late, the potential of D(2)O has been demonstrated in stabilization of the oral polio and yellow fever 17D vaccines. This review is the outcome of a thorough search and scan of the literature in a quest to explore the potential use of heavy water in the stabilization of veterinary biologicals. The literature search revealed this potential of heavy water as exemplified by successful stabilization of oral polio and yellow fever vaccines. Through this review, the authors wish to inform animal health researchers and disseminate their knowledge on the use of heavy water in biomolecule stabilization and its potential application in the stabilization of veterinary vaccines and other biologicals.

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H₂‐forming N⁵,N¹⁰‐methylenetetrahydromethanopterin dehydrogenase: mechanism of H₂ formation analyzed using hydrogen isotopes

Cited by 32 publications

References 13 publications

Reactions with Molecular Hydrogen in Microorganisms: Evidence for a Purely Organic Hydrogenation Catalyst

Reactions with Molecular Hydrogen in Microorganisms: Evidence for a Purely Organic Hydrogenation Catalyst

The role of the maturase HydG in [FeFe]‐hydrogenase active site synthesis and assembly

Role of heavy water in biological sciences with an emphasis on thermostabilization of vaccines

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