Literature DB >> 3954774

Multiple forms of sulfmyoglobin as detected by 1H nuclear magnetic resonance spectroscopy.

M J Chatfield, G N La Mar, A L Balch, J T Lecomte.   

Abstract

The proton nuclear magnetic resonance spectrum of sulfmyoglobin prepared in standard fashion reveals the presence of three forms, A, B, and C, with different chemical reactivity. Conditions for some interconversions of these forms are given. The 1H NMR spectra of the different forms show similar patterns. It appears that the differences between forms involve chemical modification on the porphyrin periphery. The altered heme can be extracted from FeIII(CN) sulfmyoglobin C to give a stable green substance.

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Year:  1986        PMID: 3954774     DOI: 10.1016/0006-291x(86)90978-2

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Three-dimensional structure of cyanomet-sulfmyoglobin C.

Authors:  S V Evans; B P Sishta; A G Mauk; G D Brayer
Journal:  Proc Natl Acad Sci U S A       Date:  1994-05-24       Impact factor: 11.205

Review 2.  Hydrogen sulfide activation in hemeproteins: the sulfheme scenario.

Authors:  Bessie B Ríos-González; Elddie M Román-Morales; Ruth Pietri; Juan López-Garriga
Journal:  J Inorg Biochem       Date:  2014-01-25       Impact factor: 4.155

  2 in total

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