caa a22 4500 605507988 CHVBK 20210128100634.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-014-1194-6 doi (NATIONALLICENCE)springer-10.1007/s00775-014-1194-6 Shifting the metallocentric molybdoenzyme paradigm: the importance of pyranopterin coordination [Elektronische Daten] [Richard Rothery, Joel Weiner] 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. SBIC, 2014 Cofactor nationallicence Electrochemistry nationallicence Electron transfer nationallicence Metallocenter assembly nationallicence AOR : Aldehyde oxidoreductase nationallicence AOR-fold : Aldehyde oxidoreductase protein fold nationallicence DMSOR : Dimethylsulfide reductase nationallicence DMSOR-fold : DMSO reductase protein fold nationallicence LUA : Last universal ancestor nationallicence Mo-bisPGD : Molybdo-bis(pyranopterin guanine dinucleotide) nationallicence Mo-PCD : Molybdo-pyranopterin cytosine dinucleotide nationallicence Mo-PPT : Molybdo-pyranopterin nationallicence Mo/W-enzymes : Mononuclear molybdenum or tungsten enzymes nationallicence NIA : Plant-type nitrate reductase nationallicence SUOX : Sulfite oxidase nationallicence SUOX-fold : Sulfite oxidase protein fold nationallicence W-bisPPT : Tungsto-bispyranopterin nationallicence XDH : Xanthine dehydrogenase nationallicence XDH-fold : Xanthine dehydrogenase protein fold nationallicence Rothery Richard Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut Weiner Joel Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 349-372 0949-8257 20:2<349 2015 20 775 https://doi.org/10.1007/s00775-014-1194-6 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-014-1194-6 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Rothery Richard Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut NATIONALLICENCE 700 1- Weiner Joel Department of Biochemistry, University of Alberta, T6G 2H7, Edmonton, AB, Canada aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 349-372 0949-8257 20:2<349 2015 20 775