Structure and function of the myoglobin containing octaethylhemin as a prosthetic group.
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TLDR
Results indicate that iron OEP serves as a prosthetic group for myoglobin with normal function, despite the significant structural and electronic difference between OEP and protoporphyrin.About:
This article is published in Journal of Biological Chemistry.The article was published on 1988-06-25 and is currently open access. It has received 29 citations till now. The article focuses on the topics: Metmyoglobin & Myoglobin.read more
Citations
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Journal ArticleDOI
Properties and reactivity of myoglobin reconstituted with chemically modified protohemin complexes.
Enrico Monzani,Gloria Alzuet,Luigi Casella,Cristina Redaelli,Cristina Bassani,Anna Maria Sanangelantoni,Michele Gullotti,Luca De Gioia,and Laura Santagostini,Francesco Chillemi +9 more
TL;DR: The increased active site accessibility of Mb-RA and Mb-H facilitates the binding and electron transfer of phenolic substrates in peroxidase-type oxidations catalyzed by the reconstituted proteins in the presence of hydrogen peroxide.
Journal ArticleDOI
From “hemoabzymes” to “hemozymes”: towards new biocatalysts for selective oxidations
TL;DR: A second generation of artificial hemoproteins or "hemozymes", some of which were found able to catalyze the stereoselective oxidation of organic compounds such as sulfides and alkenes by H2O2 and KHSO5, are found.
Book ChapterDOI
Proton NMR Spectroscopy of Model Hemes
F. Ann Walker,Ursula Simonis +1 more
TL;DR: Hemes and heme proteins are vital components of essentially every cell of every living organism and the transport of electrons in the respiratory chains of organisms as diverse as bacteria, yeasts, algae, plants, and animals.
Journal ArticleDOI
Hemozymes peroxidase activity of artificial hemoproteins constructed from the Streptomyces lividans xylanase A and iron(III)-carboxy-substituted porphyrins.
Rémy Ricoux,Roger Dubuc,Claude Dupont,Jean-Didier Maréchal,Aurore Martin,Marion Sellier,Jean-Pierre Mahy +6 more
TL;DR: A very interesting protective effect against oxidative degradation of the porphyrin was provided by the protein, as it was able to catalyze the oxidation of typical peroxidase cosubstrates such as guaiacol and o-dianisidine by H2O2.
Journal ArticleDOI
Molecular Insight into Intrinsic Heme Distortion in Ligand Binding in Hemoprotein
Saburo Neya,Masaaki Suzuki,Tyuji Hoshino,Hirotaka Ode,Kiyohiro Imai,Teruyuki Komatsu,Akira Ikezaki,Mikio Nakamura,Yuji Furutani,Hideki Kandori +9 more
TL;DR: A distinctive controlling mechanism for ligand binding by the deformed heme is demonstrated, whereby the iron atom is more attracted by the proximal histidine to reduce the affinity of exogenous ligands for the ferrous heme.
References
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Book
Hemoglobin and myoglobin in their reactions with ligands
Eraldo Antonini,Maurizio Brunori +1 more
Journal ArticleDOI
On the preparation of metalloporphyrins
Journal ArticleDOI
Structure of myoglobin refined at 2-0 A resolution. I. Crystallographic refinement of metmyoglobin from sperm whale.
TL;DR: The structure of sperm whale metmyoglobin has been refined using new intensity data to 2·0 A collected on a four-circle diffractometer starting with the original phase angles determined by isomorphous replacement with heavy atoms.
Journal ArticleDOI
An enzymic reduction system for metmyoglobin and methemoglobin, and its application to functional studies of oxygen carriers.
TL;DR: The oxygen equilibrium and the absorbance spectrum of the oxygenated form were successfully measured with myoglobin and hemoglobins A and M Boston and it was found that the addition of catalase or peroxidase was required for the complete reduction of metmyoglobin.