Journal Article Inhibition of 6-Methylsalicylic Acid Synthesis by the Antibiotic Cerulenin Get access Hiroie OHNO, Hiroie OHNO The Kitasato Institute and Kitasato UniversityShirokane, Minato-ku, Tokyo 108 Search for other works by this author on: Oxford Academic PubMed Google Scholar Tadao OHNO, Tadao OHNO The Kitasato Institute and Kitasato UniversityShirokane, Minato-ku, Tokyo 108 Search for other works by this author on: Oxford Academic PubMed Google Scholar Juichi AWAYA, Juichi AWAYA The Kitasato Institute and Kitasato UniversityShirokane, Minato-ku, Tokyo 108 Search for other works by this author on: Oxford Academic PubMed Google Scholar Satoshi ÖMURA Satoshi ÖMURA 1 The Kitasato Institute and Kitasato UniversityShirokane, Minato-ku, Tokyo 108 1 To whom all of correspondence should be addressed. Search for other works by this author on: Oxford Academic PubMed Google Scholar The Journal of Biochemistry, Volume 78, Issue 6, December 1975, Pages 1149–1152, https://doi.org/10.1093/oxfordjournals.jbchem.a131010 Published: 01 December 1975 Article history Received: 28 May 1975 Published: 01 December 1975
A highly purified non-heme iron protein has been prepared from pig testis. The protein contains iron and labile sulfide in approximately equimolar amounts. Optical absorption maxima occur at 455 mμ, 415 mμ, 320 mμ and 276 mμ with a small shoulder at 518 mμ in the oxidized form. In the reduced form, the absorption in the visible region is markedly bleached and a new maximum appears at 550 mμ. The optical rotatory dispersion and the circular dichroism spectra exhibit marked multiple Cotton effects. Upon reduction, the dispersion spectrum is greatly changed. The electron spin resonance spectrum exhibits a temperature sensitive signal at g=1.94 upon reduction. All of the properties are strikingly similar to those of adrenal non-heme iron protein (adrenodoxin) and plant ferredoxins. The substitution of the non-heme iron protein from testis for adrenodoxin in the adrenal steroid 11-β-hydroxylation reaction was accomplished, and the preparation of non-heme iron protein from ovary could also be substituted for adrenodoxin, whereas the similar preparation from liver, spinach and Euglena ferredoxins, Pseudomonas rubredoxin and putida redoxin were all inactive. The absence of adrenodoxin-like non-heme iron protein in the brain, liver, kidney and pancreas is suggested.
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTStructure of elasnin, a novel elastase inhibitor containing an .alpha.-pyrone ringAkira Nakagawa, Hiroie Ohno, Katsuji Miyano, and Satoshi OmuraCite this: J. Org. Chem. 1980, 45, 16, 3268–3274Publication Date (Print):August 1, 1980Publication History Published online1 May 2002Published inissue 1 August 1980https://pubs.acs.org/doi/10.1021/jo01304a025https://doi.org/10.1021/jo01304a025research-articleACS PublicationsRequest reuse permissionsArticle Views180Altmetric-Citations17LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-Alertsclose Get e-Alerts
