Zobrazeno 1 - 10 of 96 pro vyhledávání: '"J. H. Dawson"'
1
Magnetic circular dichroism studies of the active site heme coordination sphere of exogenous ligand-free ferric cytochrome c peroxidase from yeast: effects of sample history and pH
Autor: A E, Pond, M, Sono, E A, Elenkova, D E, McRee, D B, Goodin, A M, English, J H, Dawson
Publikováno v: Journal of inorganic biochemistry. 76(3-4)
Electronic absorption and magnetic circular dichroism (MCD) spectroscopic data at 4 degrees C are reported for exogenous ligand-free ferric forms of cytochrome c peroxidase (CCP) in comparison with two other histidine-ligated heme proteins, horseradi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8219d750db23c6c7c3936f62b9916168
https://pubmed.ncbi.nlm.nih.gov/10605835
Zobrazit plný text záznamu
2
Influence of protein environment on magnetic circular dichroism spectral properties of ferric and ferrous ligand complexes of yeast cytochrome c peroxidase
Autor: A E, Pond, M, Sono, E A, Elenkova, D B, Goodin, A M, English, J H, Dawson
Publikováno v: Biospectroscopy. 5
The addition of exogenous ligands to the ferric and ferrous states of yeast cytochrome c peroxidase (CCP) is investigated with magnetic circular dichroism (MCD) at 4 degrees C to determine the effect the protein environment may exercise on spectral p
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ab72de1b1341af22b07c93b68e8793f1
https://pubmed.ncbi.nlm.nih.gov/10512537
Zobrazit plný text záznamu
3
Uncoupling oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450-CAM. Direct observation of an intermolecular isotope effect for substrate C-H activation
Autor: S, Kadkhodayan, E D, Coulter, D M, Maryniak, T A, Bryson, J H, Dawson
Publikováno v: The Journal of biological chemistry. 270(47)
The hydroxylation of (1R)-camphor by cytochrome P450-CAM involves almost complete coupling of electron to oxygen transfer. Modifications at C-5 of camphor, the normal site of hydroxylation by P450-CAM, lead to as much as 98% uncoupling of electron an
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c50cb726b6f79b9e69a989716ff7d78a
https://pubmed.ncbi.nlm.nih.gov/7499289
Zobrazit plný text záznamu
4
Identification of nitric oxide synthase as a thiolate-ligated heme protein using magnetic circular dichroism spectroscopy. Comparison with cytochrome P-450-CAM and chloroperoxidase
Autor: M, Sono, D J, Stuehr, M, Ikeda-Saito, J H, Dawson
Publikováno v: The Journal of biological chemistry. 270(34)
Nitric oxide (NO) has recently been recognized as an important biomolecule playing diverse physiological roles. It is synthesized in several different tissues from L-Arg and O2, using NADPH as an electron donor, by a family of heme-containing catalyt
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a4cfb11b2a7aa36e78e1889eef4df1bf
https://pubmed.ncbi.nlm.nih.gov/7544348
Zobrazit plný text záznamu
5
X-ray absorption near edge studies of cytochrome P-450-CAM, chloroperoxidase, and myoglobin. Direct evidence for the electron releasing character of a cysteine thiolate proximal ligand
Autor: H I, Liu, M, Sono, S, Kadkhodayan, L P, Hager, B, Hedman, K O, Hodgson, J H, Dawson
Publikováno v: The Journal of biological chemistry. 270(18)
The low spin ferric and low and high spin ferrous forms of myoglobin, bacterial cytochrome P-450-CAM, and chloroperoxidase have been examined by Fe-K x-ray absorption edge spectroscopy. The positions of the absorption edge and the shapes of preedge a
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6f6fda216f29bc33d0c1599e302fad91
https://pubmed.ncbi.nlm.nih.gov/7737989
Zobrazit plný text záznamu

Vyhledávací nástroje:

Upřesnit hledání

Omezení vyhledávání
Plný text Recenzováno Digitální knihovna AV ČR
Zdroje