Photosynth Res. 2009 Oct;102(1):43-51. Epub 2009 Aug 13.

Purification and characterization of cytochrome c(6) from Acaryochloris marina.

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Department of Chemistry, Washington University in St. Louis, St. Louis, MO 63130-4899, USA.

Abstract

Cytochrome c(6), (cyt c(6)) a soluble monoheme electron transport protein, was isolated and characterized from the chlorophyll d-containing cyanobacterium Acaryochoris marina, the type strain MBIC11017. The protein was purified using ammonium sulfate precipitation, ion exchange and gel filtration column chromatography, and fast performance liquid chromatography. Its molecular mass and pI have been determined to be 8.87 kDa and less than 4.2, respectively, by mass spectrometry and isoelectrofocusing (IEF). The protein has an alpha helical structure as indicated by CD (circular dichroism) spectroscopy and a reduction midpoint potential (E(m)) of +327 mV versus the normal hydrogen electrode (NHE) as determined by redox potentiometry. Its potential role in electron transfer processes is discussed.

PMID:: 19680778; [PubMed - indexed for MEDLINE]

Publication Types, MeSH Terms, Substances, Grant Support

Publication Types

MeSH Terms

Substances

Cytochromes c6

Grant Support

2P41RR000954/RR/NCRR NIH HHS/United States

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