Eisenstein, Laura (1976). "Molecular tunneling in heme proteins". International Journal of Quantum Chemistry. 10 (S3): 21-27. ... "Dynamics of carbon monoxide binding by heme proteins". Science. 181 (4099): 541-543. Bibcode:1973Sci...181..541A. doi:10.1126/ ... "Tunneling in ligand binding to heme proteins". Science. 192 (4243): 1002-1004. Bibcode:1976Sci...192.1002A. doi:10.1126/science ...
Basak, Pijush; Pattanayak, Rudradip; Bhattacharyya, Maitree (2015). "Transition Metal Induced Conformational Change of Heme Proteins ... function and interactions with special interest to hemeproteins, biomolecular interaction. Bhattacharyya's most cited ...
ppm of carbon monoxide from degradation of heme proteins. 1 ppm of ammonia. Trace many hundreds of volatile organic compounds ...
ISBN 978-1-4665-0260-4. Huang, Xiongyi; Groves, John T. (2018). "Oxygen Activation and Radical Transformations in Heme Proteins ...
Sampath V, Zhao XJ, Caughey WS (Apr 27, 2001). "Anesthetic-like interactions of nitric oxide with albumin and hemeproteins. A ... Typical cases involve the nitrosylation of heme proteins like cytochromes, thereby disabling the normal enzymatic activity of ...
One diverse set of examples is the heme proteins, which consist of a porphyrin ring coordinated to iron. Iron-sulfur clusters ... Li T, Bonkovsky HL, Guo JT (March 2011). "Structural analysis of heme proteins: implications for design and prediction". BMC ...
This class of compounds includes the heme proteins hemoglobin and myoglobin. An exotic and unusual reaction occurs with PtF 6, ...
"Nature of O2 and CO binding to metalloporphyrins and heme proteins". Proceedings of the National Academy of Sciences of the ...
This is a common ligand for many hemeproteins including hemoglobin and myoglobin. Heme A in the cytochrome a portion of ...
Cytochromes are hemeproteins involved in the generation of ATP via electron transport. S. violacea contains three main types of ...
"The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins - 1st Edition". www.elsevier.com. Retrieved 3 ... Diatomics and their Interactions with Heme Proteins (Elsevier, 2008), a monograph on the subject, and Letters to a Young ...
One diverse set of examples is the heme proteins, which consist of a porphyrin ring coordinated to iron.[21] ... "Structural analysis of heme proteins: implications for design and prediction". BMC Structural Biology. 11: 13. doi:10.1186/ ...
Hemoglobin, erythrocruorin, and chlorocruorin are all globins, iron-heme proteins with a common core. Their color comes from ...
The binding of O2 by reduced (Fe2+)heme proteins involves formation of Fe(III) superoxide complex. The assay of superoxide ...
The compound is used in the preparation of models for the prosthetic group in heme proteins. It is a dark purple solid that is ...
Nitrite reacts with heme proteins and metal ions, neutralizing free radicals by nitric oxide (one of its byproducts). ...
Typical cases involve the nitrosylation of heme proteins like cytochromes, thereby disabling the normal enzymatic activity of ...
... or have receptors that bind directly to iron/heme proteins. In eukaryotes, other strategies to enhance iron solubility and ...
She received her Ph.D. in Medical Sciences with a focus on the ultrafast vibrational dynamics of heme proteins in 1994. ... The focus of the remainder of her PhD research was the ultrafast vibrational dynamics of heme proteins, the oxygen-carrying ...
In the case of ferric heme proteins, MCD is capable of determining both oxidation and spin state to a remarkably exquisite ...
Mg porphyrin gives rise to chlorophyll, Fe porphyrin to heme proteins, Ni porphyrin yields factor F-430, and Co porphyrin ...
Distal polar and steric effects in heme proteins and models" Journal of the American Chemical Society 1994, volume 116, pp. 162 ...
"Nature of O2 and CO binding to metalloporphyrins and heme proteins". Proc. Natl. Acad. Sci. U.S.A. 73 (10): 3333-7. Bibcode ...
The most commonly known and studied bioinorganic iron compounds (biological iron molecules) are the heme proteins: examples are ... 4H+ outside Although the heme proteins are the most important class of iron-containing proteins, the iron-sulfur proteins are ...
... , previously known as cytochrome a2, is a name for all cytochromes (electron-transporting heme proteins) that ...
Computer simulation of heme proteins of physiopathological relevance. ...
Some hemeproteins, often from single cell organisms, may contain five hemes C. The bc1 complex is another important enzyme that ... It is common for the heme C to amino acid ratio to be high for bacterial hemeproteins, so the interiors of some cytochrome c ... proteins appear packed with many heme C groups compared with other hemeproteins. ...
... structures and biological function of heme proteins. Emma was born in Northamptonshire and was educated in state schools at ...
He is also a pioneer in using resonance Raman spectroscopy to study heme proteins, notably hemoglobin, Cytochrome c oxidase, ...
... albeit with rate and equilibrium constants 100 to 1,000,000-fold smaller than other high-spin hemeproteins. This, coupled with ...