ArticleHigh pressure research2010
Constrained water access to the active site of cytochrome P450 from the piezophilic bacterium Photobacterium profundum.
Article in High pressure research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Role of cavities and hydration in the pressure unfolding of T4 lysozyme.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- P450cin active site water: implications for substrate binding and solvent accessibility.Biochemistry · 2013Article
- Cytochrome P450 from Photobacterium profundum SS9, a piezophilic bacterium, exhibits a tightened control of water access to the active site.Biochemistry · 2010Article
- CYP261 enzymes from deep sea bacteria: a clue to conformational heterogeneity in cytochromes P450.Biotechnology and applied biochemistryArticle
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Living species inhabiting ocean deeps must adapt to high hydrostatic pressure. This adaptation, which must enable functioning under conditions of promoted protein hydration, is especially important for proteins such as cytochromes P450 that exhibit functionally important hydration-dehydration dynamics. Here we study the interactions of substrates with cytochrome P450-SS9, a putative fatty acid hydroxylase from the piezophilic bacterium Photobacterium profundum SS9, and characterize the protein's barotropic properties. Comparison of P450-SS9 with cytochrome P450BM-3, a mesophilic fatty acid hydroxylase, suggests that P450-SS9 is characterized by severely confined accessibility and low water occupancy of the active site. This feature may reveal a mechanism of structural adaptation of the piezophilic enzyme. We also demonstrate that saturated and unsaturated fatty acids exert opposite effects on solvent accessibility and hydration of the active site. Modulation of the protein conformation by fatty acids is hypothesized to have an important physiological function in the piezophile.
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Registered trials
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