The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The anatomy of a bifunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1
Open accessAbstract
Cytochrome cd1-nitrite reductase is a bifunctional enzyme that catalyzes the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of oxygen to water. The 1.55 A crystal structure of the dimeric enzyme from Thiosphaera pantotropha is reported here. The protein was sequenced from the X-ray structure. Each subunit contains a covalent c heme with two axial His ligands (His-17, His-69) and a unique noncovalent d1 heme ligated by Tyr-25 and His-200. The d1 heme is the mononuclear iron center where both oxygen and nitrite reduction take place. The two types of heme are located in separate domains whose arrangement suggests a mechanism requiring domain movement during catalysis.
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Cites
Bacterial nitrite-reducing enzymes
BRITTAIN, T., BLACKMORE, R., GREENWOOD, C., & THOMSON, A. J. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb17350.x · Cited by 105
Cited by
Berks, B. C., Ferguson, S. J., Moir, J. W. B., & Richardson, D. J. (1995) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(95)00092-5 · Cited by 596
Self-citationMaia, L. B., & Moura, J. J. G. (2014) · Chemical Reviews · doi:10.1021/cr400518y · Cited by 401
Sarkhel, S., & Desiraju, G. R. (2004) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.10567 · Cited by 285
Heme: the most versatile redox centre in biology?
Chapman, S. K., Daff, S., & Munro, A. W. (1997) · Metal Sites in Proteins and Models · doi:10.1007/3-540-62870-3_2 · Cited by 72
Bali, S., Palmer, D. J., Schroeder, S., Ferguson, S. J., & Warren, M. J. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1563-x · Cited by 53
Metadata
- Authors
- Fülöp, V., Moir, J. W. B., Ferguson, S. J., & Hajdu, J.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1995-05
- Volume
- 81
- Issue
- 3
- Pages
- 369-377
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2013266955
- Cited by
- 268
- References
- 1
- FWCI
- 13.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Fülöp, V., Moir, J. W. B., Ferguson, S. J., & Hajdu, J. (1995). The anatomy of a bifunctional enzyme: Structural basis for reduction of oxygen to water and synthesis of nitric oxide by cytochrome cd1. Cell. https://doi.org/10.1016/0092-8674(95)90390-9
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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