Constrained water access to the active site of cytochrome P450 from the piezophilic bacterium Photobacterium profundum

Elena V. Sineva, Dmitri R. Davydov

Research output: Contribution to journalArticle

5 Citations (Scopus)

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 for the 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.

Original languageEnglish (US)
Pages (from-to)466-474
Number of pages9
JournalHigh Pressure Research
Volume30
Issue number4
DOIs
StatePublished - Dec 1 2010

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cytochromes
fatty acids
bacteria
proteins
hydration
water
dehydration
hydrostatic pressure
enzymes
oceans
modulation
interactions

All Science Journal Classification (ASJC) codes

  • Condensed Matter Physics

Cite this

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Constrained water access to the active site of cytochrome P450 from the piezophilic bacterium Photobacterium profundum. / Sineva, Elena V.; Davydov, Dmitri R.

In: High Pressure Research, Vol. 30, No. 4, 01.12.2010, p. 466-474.

Research output: Contribution to journalArticle

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