Reactions of persulfides with the heme cofactor of oxidized myoglobin and microperoxidase 11: reduction or coordination.
Sign Up to like & getrecommendations! Published in 2017 at "Dalton transactions"
DOI: 10.1039/c7dt01638g
Abstract: Persulfides of cysteine (CysSSH), glutathione (GSSH) or N-methoxycarbonyl-penicillamine (NAcPenSSH) react with the ferric form of myoglobin (metMb(iii)) to yield the oxy-ferrous (oxyMb(ii)) or deoxy-ferrous (deoxyMb(ii)) forms of myoglobin under aerobic or anaerobic conditions, respectively. Under… read more here.
Keywords: cofactor oxidized; heme cofactor; reactions persulfides; myoglobin microperoxidase ... See more keywords
A novel catalytic heme cofactor in SfmD with a single thioether bond and a bis-His ligand set revealed by a de novo crystal structural and spectroscopic study†
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DOI: 10.1039/d0sc06369j
Abstract: SfmD is a heme-dependent enzyme in the biosynthetic pathway of saframycin A. Here, we present a 1.78 Å resolution de novo crystal structure of SfmD, which unveils a novel heme cofactor attached to the protein… read more here.
Keywords: novo crystal; heme; heme cofactor; sfmd ... See more keywords
Single gold nanoparticle-driven heme cofactor nanozyme as an unprecedented oxidase mimetic.
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DOI: 10.1039/d1cc00279a
Abstract: The catalytic diversity of heme enzymes is a perpetuating pursuit for biomimetic chemistry, but heme nanozymes exhibit catalytic activity only reminiscent of peroxidases. Miraculously, the oxidase-like catalytic function of a heme cofactor is elicited with… read more here.
Keywords: heme; heme cofactor; single gold; gold nanoparticle ... See more keywords