A Spectroelectrochemical Method for Differentiation of Steric and Electronic Effects in Hemoglobins and Myoglobins
TLDR
The difference between inositol hexaphosphate effects on initial stages of oxidation and oxygenation indicates that the explanation for “multiple T states” in oxygen binding lies in the ability of the polyanion to greatly increase steric hindrance to ligand entry, without appreciable changes in the electronic features of the heme environment.About:
This article is published in Journal of Biological Chemistry.The article was published on 1995-06-09 and is currently open access. It has received 82 citations till now. The article focuses on the topics: Oxygen binding & Cooperativity.read more
Citations
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Direct Electrochemistry and Electrocatalysis of Heme Proteins Entrapped in Agarose Hydrogel Films in Room-Temperature Ionic Liquids
TL;DR: In this article, the electrochemistry and electrocatalysis of a number of heme proteins entrapped in agarose hydrogel films in the room-temperature ionic liquid 1-butyl-3-methylimidazolium hexafluorophosphate ([bmim][PF(6)]) have been investigated.
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The Reaction between Nitrite and Deoxyhemoglobin REASSESSMENT OF REACTION KINETICS AND STOICHIOMETRY
Kris T. Huang,Agnes Keszler,Neil K. Patel,Rakesh P. Patel,Mark T. Gladwin,Daniel B. Kim-Shapiro,Neil Hogg +6 more
TL;DR: The reactivity of nitrite with heme is clearly more complex than has been previously realized and is dependent upon the conformational state of the hemoglobin tetramer, suggesting that the nitrite reductase activity of hemoglobin is under allosteric control.
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Direct electrochemistry and electrocatalysis of heme-proteins entrapped in agarose hydrogel films.
TL;DR: Three heme-proteins, including myoglobin, hemoglobin and horseradish peroxidase, were immobilized on edge-plane pyrolytic graphite (EPG) electrodes by agarose hydrogel to explore the mechanisms for catalytic reduction of hydrogen peroxide and nitric oxide by proteins entrapped in agaroses hydrogels.
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The interface behavior of hemoglobin at carbon nanotube and the detection for H2O2
TL;DR: Direct electrochemistry of hemoglobin (Hb) is observed at carbon nanotube (CNT) interface and it is found that the adsorbing Hb still keeps its catalytic activity to H(2)O(2).
References
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On the Nature of Allosteric Transitions: A Plausible Model
TL;DR: "It is certain that all bodies whatsoever, though they have no sense, yet they have perception, and whether the body be alterant or alterec, evermore a perception precedeth operation; for else all bodies would be like one to another."
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Stereochemistry of cooperative effects in haemoglobin.
TL;DR: The oxygenation of haemoglobin is accompanied by structural changes in the subunits triggered by shifts of the iron atoms relative to the porphyrin and, in the β-subunits, also by the steric effect of oxygen itself.
Book
Hemoglobin and myoglobin in their reactions with ligands
Eraldo Antonini,Maurizio Brunori +1 more
Book
Handbook Methods For Oxygen Radical Research
TL;DR: The CRC handbook of methods for oxygen radical research is a guide to the development of effective and efficient methods for evaluating the properties of oxygen in the atmosphere.
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The Generation of Superoxide Radical during the Autoxidation of Hemoglobin
Hara P. Misra,Irwin Fridovich +1 more
TL;DR: Clostridial and spinach ferredoxins, reduced enzymatically by the action of ferredoxin-TPN+ oxidoreductase, have been shown to carry out the univalent reduction of oxygen.