Heme: emergent roles of heme in signal transduction, functional regulation and as catalytic centres
T Shimizu, A Lengalova, V Martínek… - Chemical Society …, 2019 - pubs.rsc.org
Protoporphyrin IX iron complex (heme) is an important cofactor for oxygen transfer, oxygen
storage, oxygen activation, and electron transfer when bound to the heme proteins …
storage, oxygen activation, and electron transfer when bound to the heme proteins …
The nature and reactivity of ferryl heme in compounds I and II
PCE Moody, EL Raven - Accounts of chemical research, 2018 - ACS Publications
Conspectus Aerobic organisms have evolved to activate oxygen from the atmosphere, which
allows them to catalyze the oxidation of different kinds of substrates. This activation of …
allows them to catalyze the oxidation of different kinds of substrates. This activation of …
Sulfide oxidation by a noncanonical pathway in red blood cells generates thiosulfate and polysulfides
A cardioprotectant at low concentrations, H 2 S is a toxin at high concentrations and inhibits
cytochrome c oxidase. A conundrum in H 2 S homeostasis is its fate in red blood cells …
cytochrome c oxidase. A conundrum in H 2 S homeostasis is its fate in red blood cells …
Potentiation of hydrogen peroxide toxicity: From catalase inhibition to stable DNA-iron complexes
Abstract Hydrogen peroxide (H 2 O 2) is unique among general toxins, because it is stable
in abiotic environments at ambient temperature and neutral pH, yet rapidly kills any type of …
in abiotic environments at ambient temperature and neutral pH, yet rapidly kills any type of …
Stereochemical Control of Redox CoII/CoIII-Cages with Switchable Cotton Effects Based on Labile-Static States
The structural dynamics of artificial assemblies, in aspects such as molecular recognition
and structural transformation, provide us with a blueprint to achieve bioinspired applications …
and structural transformation, provide us with a blueprint to achieve bioinspired applications …
Proposed ligand-centered electrocatalytic hydrogen evolution and hydrogen oxidation at a noninnocent mononuclear metal–thiolate
The noninnocent coordinatively saturated mononuclear metal–thiolate complex ReL3 (L=
diphenylphosphinobenzenethiolate) serves as an electrocatalyst for hydrogen evolution or …
diphenylphosphinobenzenethiolate) serves as an electrocatalyst for hydrogen evolution or …
Reaction of thiosulfate dehydrogenase with a substrate mimic induces dissociation of the cysteine heme ligand giving insights into the mechanism of oxidative …
Thiosulfate dehydrogenases are bacterial cytochromes that contribute to the oxidation of
inorganic sulfur. The active sites of these enzymes contain low-spin c-type heme with Cys …
inorganic sulfur. The active sites of these enzymes contain low-spin c-type heme with Cys …
Control of carotenoid biosynthesis through a heme-based cis-trans isomerase
Plants synthesize carotenoids, which are essential for plant development and survival.
These metabolites also serve as essential nutrients for human health. The biosynthetic …
These metabolites also serve as essential nutrients for human health. The biosynthetic …
Functional divergence of heme-thiolate proteins: a classification based on spectroscopic attributes
1. INTRODUCTION Heme proteins are among the most versatile players in the biological
milieu; their functions range widely and include electron transfer, catalysis, and small …
milieu; their functions range widely and include electron transfer, catalysis, and small …
A Compact Structure of Cytochrome c Trapped in a Lysine-Ligated State: Loop Refolding and Functional Implications of a Conformational Switch
It has been suggested that the alkaline form of cytochrome c (cyt c) regulates function of this
protein as an electron carrier in oxidative phosphorylation and as a peroxidase that reacts …
protein as an electron carrier in oxidative phosphorylation and as a peroxidase that reacts …