Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination
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| 024 | 7 | 0 | |a 10.1007/s00775-014-1194-6 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-014-1194-6 | ||
| 245 | 0 | 0 | |a Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination |h [Elektronische Daten] |c [Richard Rothery, Joel Weiner] |
| 520 | 3 | |a In this review, we test the hypothesis that pyranopterin coordination plays a critical role in defining substrate reactivities in the four families of mononuclear molybdenum and tungsten enzymes (Mo/W-enzymes). Enzyme families containing a single pyranopterin dithiolene chelate have been demonstrated to have reactivity towards two (sulfite oxidase, SUOX-fold) and five (xanthine dehydrogenase, XDH-fold) types of substrate, whereas the major family of enzymes containing a bis-pyranopterin dithiolene chelate (dimethylsulfoxidereductase, DMSOR-fold) is reactive towards eight types of substrate. A second bis-pyranopterin enzyme (aldehyde oxidoreductase, AOR-fold) family catalyzes a single type of reaction. The diversity of reactions catalyzed by each family correlates with active site variability, and also with the number of pyranopterins and their coordination by the protein. In the case of the AOR-fold enzymes, inflexibility of pyranopterin coordination correlates with their limited substrate specificity (oxidation of aldehydes). In examples of the SUOX-fold and DMSOR-fold enzymes, we observe three types of histidine-containing charge-transfer relays that can: (1) connect the piperazine ring of the pyranopterin to the substrate-binding site (SUOX-fold enzymes); (2) provide inter-pyranopterin communication (DMSOR-fold enzymes); and (3) connect a pyran ring oxygen to deeply buried water molecules (the DMSOR-fold NarGHI-type nitrate reductases). Finally, sequence data mining reveals a number of bacterial species whose predicted proteomes contain large numbers (up to 64) of Mo/W-enzymes, with the DMSOR-fold enzymes being dominant. These analyses also reveal an inverse correlation between Mo/W-enzyme content and pathogenicity. | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a Cofactor |2 nationallicence | |
| 690 | 7 | |a Electrochemistry |2 nationallicence | |
| 690 | 7 | |a Electron transfer |2 nationallicence | |
| 690 | 7 | |a Metallocenter assembly |2 nationallicence | |
| 690 | 7 | |a AOR : Aldehyde oxidoreductase |2 nationallicence | |
| 690 | 7 | |a AOR-fold : Aldehyde oxidoreductase protein fold |2 nationallicence | |
| 690 | 7 | |a DMSOR : Dimethylsulfide reductase |2 nationallicence | |
| 690 | 7 | |a DMSOR-fold : DMSO reductase protein fold |2 nationallicence | |
| 690 | 7 | |a LUA : Last universal ancestor |2 nationallicence | |
| 690 | 7 | |a Mo-bisPGD : Molybdo-bis(pyranopterin guanine dinucleotide) |2 nationallicence | |
| 690 | 7 | |a Mo-PCD : Molybdo-pyranopterin cytosine dinucleotide |2 nationallicence | |
| 690 | 7 | |a Mo-PPT : Molybdo-pyranopterin |2 nationallicence | |
| 690 | 7 | |a Mo/W-enzymes : Mononuclear molybdenum or tungsten enzymes |2 nationallicence | |
| 690 | 7 | |a NIA : Plant-type nitrate reductase |2 nationallicence | |
| 690 | 7 | |a SUOX : Sulfite oxidase |2 nationallicence | |
| 690 | 7 | |a SUOX-fold : Sulfite oxidase protein fold |2 nationallicence | |
| 690 | 7 | |a W-bisPPT : Tungsto-bispyranopterin |2 nationallicence | |
| 690 | 7 | |a XDH : Xanthine dehydrogenase |2 nationallicence | |
| 690 | 7 | |a XDH-fold : Xanthine dehydrogenase protein fold |2 nationallicence | |
| 700 | 1 | |a Rothery |D Richard |u Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada |4 aut | |
| 700 | 1 | |a Weiner |D Joel |u Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 349-372 |x 0949-8257 |q 20:2<349 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1194-6 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a review-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1194-6 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Rothery |D Richard |u Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Weiner |D Joel |u Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/2(2015-03-01), 349-372 |x 0949-8257 |q 20:2<349 |1 2015 |2 20 |o 775 | ||