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Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450.
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| Zeitschriftentitel: | Proceedings of the National Academy of Sciences |
|---|---|
| Personen und Körperschaften: | , |
| In: | Proceedings of the National Academy of Sciences, 73, 1976, 10, S. 3338-3342 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Proceedings of the National Academy of Sciences
|
| Schlagwörter: |
| author_facet |
Chang, C K Dolphin, D Chang, C K Dolphin, D |
|---|---|
| author |
Chang, C K Dolphin, D |
| spellingShingle |
Chang, C K Dolphin, D Proceedings of the National Academy of Sciences Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. Multidisciplinary |
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chang, c k |
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Chang, C K Dolphin, D 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.73.10.3338 <jats:p>Mercaptide anions form exclusively penta-coordinate heme complexes [RS-heme] in polar and nonpolar solution over a wide range of mercaptide concentration. These complexes have a Soret peak at 408 nm and a formation constant of about 2.5 X 10(4) M(-1), and combine with CO to give a CO-cytochrome P-450 type spectrum. Kinetics of CO binding to mercaptide-heme complexes [RS-heme] have been studied by the flash photolysis method. Characteristic constants for this reaction suggest close similarities between [CH3-(CH2)3-S-heme] and cytochrome P-450. The reaction of alkoxide anion with heme has also been examined but no evidence was found for the existence of the [RO-heme-CO[ species.</jats:p> Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. Proceedings of the National Academy of Sciences |
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Proceedings of the National Academy of Sciences, 1976 |
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| title |
Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_unstemmed |
Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_full |
Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_fullStr |
Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_full_unstemmed |
Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_short |
Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_sort |
carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome p-450. |
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Multidisciplinary |
| url |
http://dx.doi.org/10.1073/pnas.73.10.3338 |
| publishDate |
1976 |
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3338-3342 |
| description |
<jats:p>Mercaptide anions form exclusively penta-coordinate heme complexes [RS-heme] in polar and nonpolar solution over a wide range of mercaptide concentration. These complexes have a Soret peak at 408 nm and a formation constant of about 2.5 X 10(4) M(-1), and combine with CO to give a CO-cytochrome P-450 type spectrum. Kinetics of CO binding to mercaptide-heme complexes [RS-heme] have been studied by the flash photolysis method. Characteristic constants for this reaction suggest close similarities between [CH3-(CH2)3-S-heme] and cytochrome P-450. The reaction of alkoxide anion with heme has also been examined but no evidence was found for the existence of the [RO-heme-CO[ species.</jats:p> |
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| author | Chang, C K, Dolphin, D |
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| description | <jats:p>Mercaptide anions form exclusively penta-coordinate heme complexes [RS-heme] in polar and nonpolar solution over a wide range of mercaptide concentration. These complexes have a Soret peak at 408 nm and a formation constant of about 2.5 X 10(4) M(-1), and combine with CO to give a CO-cytochrome P-450 type spectrum. Kinetics of CO binding to mercaptide-heme complexes [RS-heme] have been studied by the flash photolysis method. Characteristic constants for this reaction suggest close similarities between [CH3-(CH2)3-S-heme] and cytochrome P-450. The reaction of alkoxide anion with heme has also been examined but no evidence was found for the existence of the [RO-heme-CO[ species.</jats:p> |
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| imprint | Proceedings of the National Academy of Sciences, 1976 |
| imprint_str_mv | Proceedings of the National Academy of Sciences, 1976 |
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| physical | 3338-3342 |
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| series | Proceedings of the National Academy of Sciences |
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| spelling | Chang, C K Dolphin, D 0027-8424 1091-6490 Proceedings of the National Academy of Sciences Multidisciplinary http://dx.doi.org/10.1073/pnas.73.10.3338 <jats:p>Mercaptide anions form exclusively penta-coordinate heme complexes [RS-heme] in polar and nonpolar solution over a wide range of mercaptide concentration. These complexes have a Soret peak at 408 nm and a formation constant of about 2.5 X 10(4) M(-1), and combine with CO to give a CO-cytochrome P-450 type spectrum. Kinetics of CO binding to mercaptide-heme complexes [RS-heme] have been studied by the flash photolysis method. Characteristic constants for this reaction suggest close similarities between [CH3-(CH2)3-S-heme] and cytochrome P-450. The reaction of alkoxide anion with heme has also been examined but no evidence was found for the existence of the [RO-heme-CO[ species.</jats:p> Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. Proceedings of the National Academy of Sciences |
| spellingShingle | Chang, C K, Dolphin, D, Proceedings of the National Academy of Sciences, Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450., Multidisciplinary |
| title | Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_full | Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_fullStr | Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_full_unstemmed | Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_short | Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| title_sort | carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome p-450. |
| title_unstemmed | Carbon monoxide binding to pentacoordinate mercaptide-heme complexes: kinetic study on models for cytochrome P-450. |
| topic | Multidisciplinary |
| url | http://dx.doi.org/10.1073/pnas.73.10.3338 |