Apoprotein formation and heme reconstitution of cytochrome P-450cam.

G. C. Wagner, M. Perez, W. A. Toscano, I. C. Gunsalus

Research output: Contribution to journalArticle

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Abstract

Apoprotein suitable for heme reconstitution has been prepared by an acid/butanone extraction of cytochrome P-450cam at pH 2.5. Absorption spectra of apo-P-450cam indicate less than 2% residual holoenzyme. Four tryptophan residues per molecule were estimated from the aromatic absorbance region of denatured apoprotein. Heme-reconstituted holoprotein was purified in 30% yield to a specific activity equivalent to the native enzyme. Absorption and EPR spectra of 57Fe- and 54Fe-heme-enriched P-450cam reveal complete restoration of the native active site.

Original languageEnglish (US)
Pages (from-to)6262-6265
Number of pages4
JournalJournal of Biological Chemistry
Volume256
Issue number12
StatePublished - Jun 25 1981

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