The DOI matches its Crossref record; 22 of the 22 references it cites were found in a registry or an index.
The Structure of cbb 3 Cytochrome Oxidase Provides Insights into Proton Pumping
Abstract
C-Family Oxidase Structure: The heme-copper oxidases (HCOs) play a key role in aerobic respiration by coupling oxygen reduction to transmembrane proton pumping to generate electrochemical ion gradients across biological membranes that provide energy for many cellular processes. Based on subunit composition, electron donor, and heme type, the HCOs are divided into three families, of which families A and B have been structurally characterized. Buschmann et al. (p. 327 , published online 24 June) now report the crystal structure of the C-family cbb3 oxidase from Pseudomonas stutzeri . The structure suggests a different redox-driven pumping mechanism from A and B HCOs, and gives insight into why C HCOs are catalytically active at low oxygen concentrations.
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Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M., Kieber-Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,751
Reaction Mechanism of Cytochrome c Oxidase
Yoshikawa, S., & Shimada, A. (2015) · Chemical Reviews · doi:10.1021/cr500266a · Cited by 481
Protein Design: Toward Functional Metalloenzymes
Yu, F., Cangelosi, V. M., Zastrow, M. L., Tegoni, M., Plegaria, J. S., Tebo, A. G., Mocny, C. S., Ruckthong, L., Qayyum, H., & Pecoraro, V. L. (2014) · Chemical Reviews · doi:10.1021/cr400458x · Cited by 441
Structural Basis of Biological N 2 O Generation by Bacterial Nitric Oxide Reductase
Hino, T., Matsumoto, Y., Nagano, S., Sugimoto, H., Fukumori, Y., Murata, T., Iwata, S., & Shiro, Y. (2010) · Science · doi:10.1126/science.1195591 · Cited by 330
Architecture of bacterial respiratory chains
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Metadata
- Authors
- Buschmann, S., Warkentin, E., Xie, H., Langer, J. D., Ermler, U., & Michel, H.
- Venue
- Science
- Published
- 2010-07-16
- Volume
- 329
- Issue
- 5989
- Pages
- 327-330
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2031286484
- Cited by
- 254
- References
- 22
- FWCI
- 14.95
- Type
- journal article
- Language
- en
- Open access
- closed
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