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

Chatfield, Mariann J.; Mar, Gerd N. La; Balch, Alan L.; Lecomte, Juliette T. J.

doi:10.1016/0006-291x(86)90978-2

Cited by 27 publications

(26 citation statements)

References 12 publications

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“…The major resonances observed in this spectrum correspond with those previously found for sulphMb [6,10], but some differences are apparent. In previous reports [6,10], three isomeric forms of sulphMb were identified, SAMb, &Mb and &Mb. The relative amounts of these components depend on oxidation state, solution pH, chromatographic methods employed and the age of the sample.…”

Section: Na4r Spectroscopysupporting

confidence: 86%

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Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli

Lloyd

Mauk

1994

FEBS Letters

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Expression of recombinant horse heart myoglobin in Escherichia coli has been found to result in the production of both native and variable amounts (-1617% total) of two sulphmyoglobin isomers. The recombinant sulphmyoglobin produced consists primarily of the A and B isomers as identified by 'H NMR spectroscopy with no evidence for production of the C isomer. Conversion of recombinant sulphmyoglobin to the native protein can be achieved by reconstitution with protohaem IX. The possible relationship of this observation to recombinant expression of other heme proteins is discussed.

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Section: Na4r Spectroscopysupporting

confidence: 86%

“…1 B [lo]. Under basic conditions decay of SAMb yields mainly &Mb, the thermodynamically stable product [6,7,10], which has been shown to contain a chlorin prosthetic group in which the vinyl group of pyrole II has formed an exocyclic thiolene ring [8,9], Fig. 1C.…”

Section: Metmb + H202 + Ferrylmb Ferrylmb + Hs + Fe(iii)sulphmbmentioning

confidence: 99%

Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli

Lloyd

Mauk

1994

FEBS Letters

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“…Proton NMR studies of several sulfMbCN complexes revealed that there are at least three isomeric forms of the chlorin structure that may affects O 2 affinity [29, 30]. As shown in Figure 4b, each sulfheme isomer, named sulfMbA, sulfMbB and sulfMbC, have different chemical properties and hence, different reactivity and stability [29, 34].…”

Section: Interaction Of H2s With Myoglobin and Hemoglobinmentioning

confidence: 99%

“…As shown in Figure 4b, each sulfheme isomer, named sulfMbA, sulfMbB and sulfMbC, have different chemical properties and hence, different reactivity and stability [29, 34]. These differences reside in the porphyrin periphery alterations where the incorporated sulfur lays since all three isomers where observed at different pH, temperature and protein concentration [29]. In general, the NMR spectra of all isomers showed symmetry reduction of the prosthetic group and alteration of the π conjugation of pyrrole B [34].…”

Section: Interaction Of H2s With Myoglobin and Hemoglobinmentioning

confidence: 99%

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Ríos-González¹,

Román-Morales²,

Pietri³

et al. 2014

Journal of Inorganic Biochemistry

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Traditionally known as a toxic gas, hydrogen sulfide (H2S) is now recognized as an important biological molecule involved in numerous physiological functions. Like nitric oxide (•NO) and carbon monoxide (CO), H2S is produced endogenously in tissues and cells and can modulate biological processes by acting on target proteins. For example, interaction of H2S with the oxygenated form of human hemoglobin and myoglobin produces a sulfheme protein complex that has been implicated in H2S degradation. The presence of this sulfheme derivative has also been used as a marker for endogenous H2S synthesis and metabolism. Remarkably, human catalases and peroxidases also generate this sulfheme product. In this review, we describe the structural and functional aspects of the sulfheme derivative in these proteins and postulate a generalized mechanism for sulfheme protein formation. We also evaluate the possible physiological function of this complex and highlight the issues that remain to be assessed to determine the role of sulheme proteins in H2S metabolism, detection and physiology.

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“…NMR studies have established that there are at least three forms of SMb. The form initially produced, SAMb, is converted in acidic solution to SBMb or, in basic medium, to ScMb (15,16). SCMb is the most stable of these derivatives and has been suggested by subsequent NMR studies to possess a prosthetic group with a structure similar to that shown in Fig.…”

mentioning

confidence: 99%

Three-dimensional structure of cyanomet-sulfmyoglobin C.

Evans

Sishta²,

Mauk³

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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The atomic structure of horse heart cyanomet-sulfmyoglobin C has been establied by x-ray crystalographic techniques to a resolution of 2.0 A with an R value of 0.129. The protoheme IX prosthetic group of this thermodynamically stable sulfnyoglobin derivative has been converted to a chlorin in which the pyrrole ring bearing the 4-vinyl group is saturated and possesses an exocyclic thiolene ring. This study provides the three-dimensional structure of a protein with an iron-chlorin prosthetic group. The overall conformation of the surrounding polypeptide chain of the modified protein is very similar to that of the native protein. However, the addition of the sufuratom has caused a distortion of the prosthetic group from that in the native protein to result in the repositioning of the side chains of some residues in the heme pocket.

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

Cited by 27 publications

References 12 publications

Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli

Formation of sulphmyoglobin during expression of horse heart myoglobin in Escherichia coli

Hydrogen sulfide activation in hemeproteins: The sulfheme scenario

Three-dimensional structure of cyanomet-sulfmyoglobin C.

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