The bio-inorganic chemistry of tungsten

Hagen, W.R.; Arendsen, A.F.

doi:10.1007/3-540-62888-6_6

Cited by 42 publications

(37 citation statements)

References 128 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In contrast, D. gigas Fdh [3] and Fdh enzymes from Syntrophobacter fumaroxidans incorporate W [5], despite their growth with enough Mo in the medium. These examples suggest that bioavailability is not the only condition for an enzyme to incorporate either Mo or W and that some enzymes can function only with a specific ion, as in the case of the W-Fdh described above, the W enzymes found in hyperthermofilic archaea [2,6], and the Mo-AOR from SRB. desulfuricans NapA is shown in blue, R. sphaeroides NapAB in gray, E. coli Fdh-H in red, E. coli Fdh-N in gold, and D. gigas WFdh in yellow.…”

Section: Incorporation Of Either Mo or W In Enzymesmentioning

confidence: 99%

“…Redox properties. W-containing enzymes generally catalyze reactions with low redox potentials ( £ )420 mV) [2,6]. In the case of W-Fdh enzymes, these were also shown to catalyze the conversion of CO 2 to formate [5], a fact not yet demonstrated in any Mo-Fdh.…”

Section: Incorporation Of Either Mo or W In Enzymesmentioning

confidence: 99%

“…Mo-containing enzymes are found in almost all forms of life [1], whereas W-containing enzymes seem to be exclusive for organisms such as hyperthermofilic archaea that live in extreme environments [2]. However, W-containing enzymes have been found in organisms that do not need extreme conditions [3,4,5], suggesting a more important role for tungsten [6]. Some of the mononuclear W-containing enzymes described present active sites similar to the Mo enzymes, but they have different 3D structures and have been classified in a different group [2,7].…”

mentioning

confidence: 99%

See 2 more Smart Citations

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

et al. 2004

View full text Add to dashboard Cite

Molybdenum and tungsten are second-and third-row transition elements, respectively, which are found in a mononuclear form in the active site of a diverse group of enzymes that generally catalyze oxygen atom transfer reactions. Mononuclear Mo-containing enzymes have been classified into three families: xanthine oxidase, DMSO reductase, and sulfite oxidase. The proteins of the DMSO reductase family present the widest diversity of properties among its members and our knowledge about this family was greatly broadened by the study of the enzymes nitrate reductase and formate dehydrogenase, obtained from different sources. We discuss in this review the information of the better characterized examples of these two types of Mo enzymes and W enzymes closely related to the members of the DMSO reductase family. We briefly summarize, also, the few cases reported so far for enzymes that can function either with Mo or W at their active site.

show abstract

Section: Incorporation Of Either Mo or W In Enzymesmentioning

confidence: 99%

Section: Incorporation Of Either Mo or W In Enzymesmentioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Mo and W bis-MGD enzymes: nitrate reductases and formate dehydrogenases

et al. 2004

View full text Add to dashboard Cite

show abstract

“…In a similar vein, the active centers in tungsten-containing enzymes such as aldehyde oxidoreductase and formate dehydrogenase [55,56] have been modeled using a variety of Tp RR 0 complexes [52,57], as exemplified by an ene-1,2-dithiolate complex (Fig. 5) described by Young and coworkers [58].…”

Section: Tris(pyrazolyl)boratesmentioning

confidence: 98%

Synthetic Bioinorganic Chemistry: Scorpionates Turn 50

Rabinovich

2016

Structure and Bonding

View full text Add to dashboard Cite

The coordination chemistry of scorpionates, anionic tripodal boroncentered ligands that readily bind to virtually all main group, transition, and f-block metals, has had a profound effect in the development of synthetic bioinorganic chemistry during the past 50 years. Highlighted in this article are some of the most meaningful results published in the area, primarily in the preparation of structural and functional model compounds for the active sites in metalloproteins and metalloenzymes, a theme that encompasses topics as diverse as nitrogen fixation and heavy metal poisoning. It has also been 50 years since the genesis of Structure and Bonding, so let this account also be a celebration of the many contributions that the staunch serial has had on the entire field of inorganic chemistry during the past half century.

show abstract

“…A variety of chemical reactions such as hydrodesulfurization, oxygen transfer reactions (e.g., olefin epoxidation), and olefin metathesis are catalyzed by molybdenum coordination complexes. [10][11][12][13][14][15] The useful role of molybdenum is not restricted to industrial catalysis alone: nature has also incorporated the molybdenum center in various redox enzymes such as Xanthine oxidase and DMSO reductase, in which the role of molybdenum that catalyzes a variety of net oxygen atom transfer is interesting in oxomolybdenum chemistry and much of the coordination chemistry of higher oxidation state molybdenum is found in class of complexes containing terminal (Mo＝O) and bridging (Mo-O-Mo) oxo ligands. In all of these industrial and biological reactions, molybdenum plays the role of a catalytic site.…”

Section: Introductionmentioning

confidence: 99%