Results 181 to 190 of about 2,605 (236)

Spectroelectrochemical study of the extremophilic hemeprotein HGbI (Hell's Gate Globin I)

, 2020
Luiz Antonio Gonçalves Rodrigues de Souza
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Previously unrecognized and potentially consequential challenges facing Hsp90 inhibitors in cancer clinical trials. [PDF]

Cell Stress Chaperones
Chang C, Tang X, Woodley DT, Chen M, Li W.   +4 more
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Nitric oxide regulates cytochrome P450 2D6 and 3A4 activity via concentration-dependent modulation of heme loading. [PDF]

J Biol Chem
Das Sinha P, Islam S, Biswas P, Stuehr DJ.   +3 more
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Peroxynitrite detoxification by Trypanosoma cruzi heme peroxidase supports parasite survival in macrophages. [PDF]

J Biol Chem
Skafar V, Abboud M, Freeman SL, Martínez A, Raven EL, Radi R, Piacenza L.   +6 more
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Tryptophan fluorescence of hemeproteins

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Theory of hemeprotein reactivity

Journal of Theoretical Biology, 1971
Abstract A chemical theory of hemeprotein reactivity is presented. It is based upon recent chemical and spectroscopic studies of metalloporphyrins and hemeproteins and upon the established X-ray structures of the iron (III) complexes of hemoglobin, myoglobin and cytochrome c.
C. E. Castro
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Rate Theories and Puzzles of Hemeprotein Kinetics

Science, 1985
The binding of dioxygen and carbon monoxide to heme proteins such as myoglobin and hemoglobin has been studied with flash photolysis. At temperatures below 200 K, binding occurs from within the heme pocket and, contrary to expectation, with nearly equal rates for both ligands. This observation has led to a reexamination of the theory of the association
H, Frauenfelder, P G, Wolynes
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Protein Fluctuations and Hemeprotein Affinity for Ligand

1986
Binding processes in hemeproteins involve the iron atom and the protein properties: structural and dynamics. Crystallographic data of Perutz have given an appreciate popularity to a correlation between the displacement of the iron out of the porphyrin plane and the affinity of the hemeprotein for ligand.
B. Alpert
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Optical rotatory dispersion of a respiratory hemeprotein of Chrinomus thummi

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1968
Abstract The spatial structure of an O 2 -binding hemeprotein obtained from Chironomus thummi is compared with that of sperm whale myoglobin by means of rotatory dispersion. The optical rotation at the 233-mμ minimum of the ultraviolet Cotton effect is only 70% of the value obtained for myoglobin.
H, Formanek, J, Engel
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Hemeproteins as Targets for Sulfide Species

Antioxidants & Redox Signaling, 2020
Significance: Sulfides are endogenous and ubiquitous signaling species that share the hemeproteins as biochemical targets with O2, nitric oxide, and carbon monoxide. The description of the binding mechanisms is mandatory to anticipate the biochemical relevance of the interaction.
Boubeta, Fernando Martín, Bieza, Silvina Andrea, Bringas, Mauro, Palermo, Juan Cruz, Boechi, Leonardo, Estrin, Dario Ariel, Bari, Sara Elizabeth   +6 more
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