Interactions of reactive sulfur species with metalloproteins

• Published in: Redox biology Vol. 60; p. 102617
• Main Authors: Domán, Andrea, Dóka, Éva, Garai, Dorottya, Bogdándi, Virág, Balla, György, Balla, József, Nagy, Péter
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.04.2023; Elsevier
• Subjects: from the Special Issue on Recent advances in sulfur biology and chemistry, Edited by: Dr. Peter Nagy; Heme; Hydrogen Peroxide; Hydrogen sulfide; Hydrogen Sulfide - metabolism; Metalloprotein; Metalloproteins; Oxidative stress; Oxygen - metabolism; Reactive Oxygen Species - metabolism; Reactive sulfur species; Sulfur - metabolism; Hydrogen sulfide; Oxidative stress; Reactive sulfur species; Metalloprotein; Heme
• ISSN: 2213-2317; 2213-2317
• DOI: 10.1016/j.redox.2023.102617

Reactive sulfur species (RSS) entail a diverse family of sulfur derivatives that have emerged as important effector molecules in H2S-mediated biological events. RSS (including H2S) can exert their biological roles via widespread interactions with metalloproteins. Metalloproteins are essential components along the metabolic route of oxygen in the body, from the transport and storage of O2, through cellular respiration, to the maintenance of redox homeostasis by elimination of reactive oxygen species (ROS). Moreover, heme peroxidases contribute to immune defense by killing pathogens using oxygen-derived H2O2 as a precursor for stronger oxidants. Coordination and redox reactions with metal centers are primary means of RSS to alter fundamental cellular functions. In addition to RSS-mediated metalloprotein functions, the reduction of high-valent metal centers by RSS results in radical formation and opens the way for subsequent per- and polysulfide formation, which may have implications in cellular protection against oxidative stress and in redox signaling. Furthermore, recent findings pointed out the potential role of RSS as substrates for mitochondrial energy production and their cytoprotective capacity, with the involvement of metalloproteins. The current review summarizes the interactions of RSS with protein metal centers and their biological implications with special emphasis on mechanistic aspects, sulfide-mediated signaling, and pathophysiological consequences. A deeper understanding of the biological actions of reactive sulfur species on a molecular level is primordial in H2S-related drug development and the advancement of redox medicine. [Display omitted] •Interactions with metalloproteins is a major pathway of H2S bioactivity.•Reactive sulfur species (RSS) act as effector molecules in H2S-mediated events.•Heme proteins are main targets of H2S via coordination and redox exchanges.•H2S and RSS affect oxygen transport, storage, respiration, and immune defense.•RSS and metalloproteins cooperate in cytoprotection against oxidative stress.