ArticleExtremophiles : life under extreme conditions2009
A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential.
Article in Extremophiles : life under extreme conditions, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 8 citations in OpenAlex.
- HFrontiers in microbiology · 2025Review
- Differences in Bioenergetic Metabolism of Obligately AlkaliphilicFrontiers in microbiology · 2022Review
- Formation of Proton Motive Force Under Low-Aeration Alkaline Conditions in Alkaliphilic Bacteria.Frontiers in microbiology · 2018Review
- Contribution of intracellular negative ion capacity to Donnan effect across the membrane in alkaliphilic Bacillus spp.Journal of bioenergetics and biomembranes · 2016Article
- Bioenergetics and the role of soluble cytochromes C for alkaline adaptation in gram-negative alkaliphilic Pseudomonas.BioMed research international · 2015Review
- Relationship between rates of respiratory proton extrusion and ATP synthesis in obligately alkaliphilic Bacillus clarkii DSM 8720(T).Journal of bioenergetics and biomembranes · 2012Article
- Physiological function of soluble cytochrome c-552 from alkaliphilic Pseudomonas alcaliphila AL15-21(T).Journal of bioenergetics and biomembranes · 2011Article
- The obligate alkaliphile Bacillus clarkii K24-1U retains extruded protons at the beginning of respiration.Journal of bioenergetics and biomembranes · 2010Article
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Authors and funding
13 authors at 3 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
A membrane-anchored cytochrome c-550, which is highly expressed in obligately alkaliphilic Bacillus clarkii K24-1U, was purified and characterized. The protein contained a conspicuous sequence of Gly(22)-Asn(34), in comparison with the other Bacillus small cytochromes c. Analytical data indicated that the original and lipase-treated intermediate forms of cytochrome c-550 bind to fatty acids of C(15), C(16) and C(17) chain lengths and C(15) chain length, respectively, and it was considered that these fatty acids are bound to glycerol-Cys(18). Since there was a possibility that the presence of a diacylglycerol anchor contributed to the formation of dimeric states of this protein (20 and 17 kDa in SDS-PAGE), a C18M (Cys(18) --> Met)-cytochrome c-550 was constructed. The molecular mass of the C18M-cytochrome c-550 was determined as 15 and 10 kDa in SDS-PAGE and 23 kDa in blue native PAGE. The C18M-cytochrome c-550 bound with or without Triton X-100 formed a tetramer as the original cytochrome c-550 bound with Triton X-100, as determined by gel filtration. The midpoint redox potential of cytochrome c-550 as determined by redox titration was +83 mV, while that determined by cyclic voltammetric measurement was +7 mV. The above results indicate that cytochrome c-550 is a novel cytochrome c.
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