The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
The prokaryotic complex iron–sulfur molybdoenzyme family
Open accessAbstract
Bacterial genomes encode an extensive range of respiratory enzymes that enable respiratory metabolism with a diverse group of reducing and oxidizing substrates under both aerobic and anaerobic growth conditions. An important class of enzymes that contributes to this broad diversity is the complex iron-sulfur molybdoenzyme (CISM) family. The architecture of this class comprises the following subunits. (i) A molybdo-bis(pyranopterin guanine dinucleotide) (Mo-bisPGD) cofactor-containing catalytic subunit that also contains a cubane [Fe-S] cluster (FS0). (ii) A four-cluster protein (FCP) subunit that contains 4 cubane [Fe-S] clusters (FS1-FS4). (iii) A membrane anchor protein (MAP) subunit which anchors the catalytic and FCP subunits to the cytoplasmic membrane. In this review, we define the CISM family of enzymes on the basis of emerging structural and bioinformatic data, and show that the catalytic and FCP subunit architectures appear in a wide range of bacterial redox enzymes. We evaluate evolutionary events involving genes encoding the CISM catalytic subunit that resulted in the emergence of the complex I (NADH:ubiquinone oxidoreductase) Nqo3/NuoG subunit architecture. We also trace a series of evolutionary events leading from a primordial Cys-containing peptide to the FCP architecture. Finally, many of the CISM archetypes and related enzymes rely on the tat translocon to transport fully folded monomeric or dimeric subunits across the cytoplasmic membrane. We have used genome sequence data to establish that there is a bias against the presence of soluble periplasmic molybdoenzymes in bacteria lacking an outer membrane.
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Cites
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
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“In contrast to what is observed in the MAP subunits of the succinate:ubiquinone oxidoreductases [88–91], no CISM MAP subunits are currently known that contain only a single heme.”
ResultStructure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus
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Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
Dias, J. M., Than, M. E., Humm, A., Huber, R., Bourenkov, G. P., Bartunik, H. D., Bursakov, S., Calvete, J., Caldeira, J., Carneiro, C., et al. (1999) · Structure · doi:10.1016/s0969-2126(99)80010-0 · Cited by 286
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Cited by
The mononuclear molybdenum enzymes
Hille, R., Hall, J., & Basu, P. (2014) · Chemical Reviews · doi:10.1021/cr400443z · Cited by 1,738
Molybdenum cofactors, enzymes and pathways
Schwarz, G., Mendel, R. R., & Ribbe, M. W. (2009) · Nature · doi:10.1038/nature08302 · Cited by 872
Expanded metabolic versatility of ubiquitous nitrite-oxidizing bacteria from the genus Nitrospira
Koch, H., Lücker, S., Albertsen, M., Kitzinger, K., Herbold, C., Spieck, E., Nielsen, P. H., Wagner, M., & Daims, H. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1506533112 · Cited by 549
Unifying concepts in anaerobic respiration: Insights from dissimilatory sulfur metabolism
Grein, F., Ramos, A. R., Venceslau, S. S., & Pereira, I. A. C. (2013) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.09.001 · Cited by 200
Biochemistry of catabolic reductive dehalogenation
Fincker, M., & Spormann, A. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044829 · Cited by 166
Metadata
- Authors
- Rothery, R. A., Workun, G. J., & Weiner, J. H.
- Venue
- Biochimica et Biophysica Acta (BBA) - Biomembranes
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 1778
- Issue
- 9
- Pages
- 1897-1929
- ISSN
- 0005-2736 (ISSN-L)
- OpenAlex
- W2006615663
- Cited by
- 225
- References
- 10
- FWCI
- 4.10
- Type
- journal article
- Language
- en
- Open access
- bronze
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