The reactions of hydropersulfides (RSSH) with myoglobin

L Álvarez, VS Vega, C McGinity, VS Khodade… - Archives of biochemistry …, 2020 - Elsevier
Hydropersulfides are reported to be good biological reductants, superior to thiols and akin to
selenols. As such, they have been previously shown to reduce metalloproteins such as ferric …

Sulfheme proteins: IV. The stoichiometry of sulfur incorporation and the isolation of sulfhemin, the prosthetic group of sulfmyoglobin

JA Berzofsky, J Peisach, BL Horecker - Journal of Biological Chemistry, 1972 - ASBMB
The ferrous form of sulfmyoglobin was isolated as the first stable product of the reaction of a
single mole of inorganic sulfide with 1 mole of the higher oxidation state derivative of …

The reactivity of thiol compounds with different redox states of leghaemoglobin: evidence for competing reduction and addition pathways

A Puppo, MJ Davies - Biochimica et Biophysica Acta (BBA)-Protein …, 1995 - Elsevier
Reaction of the ferric form of leghaemoglobin with hydrogen peroxide has been previously
shown to give rise to an iron (IV)-oxo (ferryl) species, and a protein radical. Inclusion of a …

[9] Thiyl radical formation during thiol oxidation by ferrylmyoglobin

E Cadenas - Methods in Enzymology, 1995 - Elsevier
Publisher Summary This chapter discusses the molecular mechanisms and methodological
aspects of the reaction of two major classes of sulfur compounds—namely, aliphatic …

The reversion to haemoglobin of sulphhaemoglobin and its coordination derivatives

EA Johnson - Biochimica et Biophysica Acta (BBA)-Protein Structure, 1970 - Elsevier
1. The progress of the formation of sulphhaemoglobin from oxyhaemoglobin and sulphide
depends on the availability of oxygen. In the absence of excess oxygen, much of the …

EPR detection of sulfanyl radical during sulfhemoglobin formation–Influence of catalase

AC Mot, C Puscas, SA Dorneanu… - Free Radical Biology …, 2019 - Elsevier
Hemoglobin in its ferryl form oxidizes hydrogen sulfide and is transformed to
sulfhemoglobin, where the sulfur is inserted covalently at the heme edge. Shown here is …

1H nuclear magnetic resonance study of the prosthetic group in sulfhemoglobin

MJ Chatfield, GN La Mar - Archives of biochemistry and biophysics, 1992 - Elsevier
The molecular and electronic structure of the modified prosthetic group of sulfhemoglobin
(SHb) was investigated by 1 H NMR for the low-spin ferric cyano-met and high-spin ferrous …

Protein sulfhydryls are protected from irreversible oxidation by conversion to mixed disulfides

C Coan, JY Ji, K Hideg, RJ Mehlhorn - Archives of biochemistry and …, 1992 - Elsevier
Protein mixed thioselenides formed by reaction of sarcoplasmic reticulum (SR) with
diselenide biradical spin labels were quantified by ESR. Whereas the reaction of SR …

Identification of the altered pyrrole in sulfmyoglobin and an extractable sulfhemin: participation of the 4-vinyl group in the saturation of the pyrrole in one form of …

MJ Chatfield, GN La Mar, JTJ Lecomte… - Journal of the …, 1986 - ACS Publications
• CO OH R")—(" D 70/30) and subsequent NMR analysis showed that 1 and 2 are mainly of
the threoconfiguration, the threo/erythro ratio being 88: 12 in both cases. The configuration …

On the combinations of methæmoglobin with H2S

D Keilin - Proceedings of the Royal Society of London …, 1933 - royalsocietypublishing.org
Seventy years ago Hoppe-Seyler (1863) found that if a current of H2S is passed through a
solution of oxyhæmoglobin a distinct adsorption band appears in the red end of the …