Spectroscopic studies on heme d in the visible and infrared

Mark R. Vavra, Russell Timkovich, Flordeliza Yap, Robert B. Gennis

Research output: Contribution to journalArticlepeer-review


Heme d has been isolated from the terminal oxidase complex of Escherichia coli strain MR43L F152 and purified by high-pressure liquid chromatography. The infrared spectrum indicated that carbonyls in the chlorin skeleton of this isolated heme existed as carboxylic acids. Earlier work on the iron-free chlorin had demonstrated the presence of a spirolactone substituent. This may have arisen from a cyclization reaction from a dicarboxylic acid, diol precursor. Although the free heme in extracts can exist as a diol, this does not prove that the diol as such is the precise form in the enzyme complex. Visible and fluorescence spectra are reported for a variety of derivatives and complexes of heme d to establish a spectral library that may be used to prove the presence of this structure in other enzymes or cells. Association constants have been measured for complexes of heme d with cyanide, imidazole, and pyridine and are contrasted to available data for protoheme.

Original languageEnglish (US)
Pages (from-to)461-468
Number of pages8
JournalArchives of Biochemistry and Biophysics
Issue number2
StatePublished - Nov 1 1986
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology


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