Eintrag weiter verarbeiten
Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands
Gespeichert in:
| Zeitschriftentitel: | Biochemical Journal |
|---|---|
| Personen und Körperschaften: | , , , , |
| In: | Biochemical Journal, 270, 1990, 2, S. 413-417 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
|
| Schlagwörter: |
| author_facet |
Berry, M J George, S J Thomson, A J Santos, H Turner, D L Berry, M J George, S J Thomson, A J Santos, H Turner, D L |
|---|---|
| author |
Berry, M J George, S J Thomson, A J Santos, H Turner, D L |
| spellingShingle |
Berry, M J George, S J Thomson, A J Santos, H Turner, D L Biochemical Journal Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands Cell Biology Molecular Biology Biochemistry |
| author_sort |
berry, m j |
| spelling |
Berry, M J George, S J Thomson, A J Santos, H Turner, D L 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2700413 <jats:p>Cytochrome c″ (Methylophilus methylotrophus) is a soluble protein, Mr 15,000, possessing one haem which is high-spin in the reduced state but switches to a low-spin form on oxidation. Low-temperature electron-paramagnetic-resonance spectroscopy of the oxidized state shows a low-spin signal at gz = 3.65 with a folded line-shape typical of a haem of low rhombicity, and the near-infrared magnetic-circular-dichroism (m.c.d.) spectra reveal an unusually intense (delta epsilon = 400 M-1.cm-1 at 5 T, 4.2 K) charge-transfer band at 1560 nm, establishing that the oxidized haem is co-ordinated by two His residues in a near-perpendicular orientation. This conformation is well established for transmembrane b cytochromes, but this appears to be the first example in a water-soluble cytochrome. The low-temperature m.c.d. spectra of the reduced form of the protein confirms that the haem contains a high-spin Fe2+ ligated by one His residue. The redox-linked spin-state change releases a His group. Since this residue is likely to bind a proton at pH values less than 6.5, this cytochrome may provide a useful model of a molecular mechanism of a redox-linked proton uptake and release process.</jats:p> Cytochrome <i>c</i>″ isolated from <i>Methylophilus methylotrophus</i>. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands Biochemical Journal |
| doi_str_mv |
10.1042/bj2700413 |
| facet_avail |
Online Free |
| finc_class_facet |
Chemie und Pharmazie Biologie |
| format |
ElectronicArticle |
| fullrecord |
blob:ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajI3MDA0MTM |
| id |
ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajI3MDA0MTM |
| institution |
DE-Gla1 DE-Zi4 DE-15 DE-Pl11 DE-Rs1 DE-105 DE-14 DE-Ch1 DE-L229 DE-D275 DE-Bn3 DE-Brt1 DE-Zwi2 DE-D161 |
| imprint |
Portland Press Ltd., 1990 |
| imprint_str_mv |
Portland Press Ltd., 1990 |
| issn |
0264-6021 1470-8728 |
| issn_str_mv |
0264-6021 1470-8728 |
| language |
English |
| mega_collection |
Portland Press Ltd. (CrossRef) |
| match_str |
berry1990cytochromecisolatedfrommethylophilusmethylotrophusanexampleofbishistidinecoordinatedfe3haemwithnearperpendicularorientationoftheligands |
| publishDateSort |
1990 |
| publisher |
Portland Press Ltd. |
| recordtype |
ai |
| record_format |
ai |
| series |
Biochemical Journal |
| source_id |
49 |
| title |
Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_unstemmed |
Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_full |
Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_fullStr |
Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_full_unstemmed |
Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_short |
Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_sort |
cytochrome <i>c</i>″ isolated from <i>methylophilus methylotrophus</i>. an example of bis-histidine-co-ordinated fe3+ haem, with near-perpendicular orientation of the ligands |
| topic |
Cell Biology Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1042/bj2700413 |
| publishDate |
1990 |
| physical |
413-417 |
| description |
<jats:p>Cytochrome c″ (Methylophilus methylotrophus) is a soluble protein, Mr 15,000, possessing one haem which is high-spin in the reduced state but switches to a low-spin form on oxidation. Low-temperature electron-paramagnetic-resonance spectroscopy of the oxidized state shows a low-spin signal at gz = 3.65 with a folded line-shape typical of a haem of low rhombicity, and the near-infrared magnetic-circular-dichroism (m.c.d.) spectra reveal an unusually intense (delta epsilon = 400 M-1.cm-1 at 5 T, 4.2 K) charge-transfer band at 1560 nm, establishing that the oxidized haem is co-ordinated by two His residues in a near-perpendicular orientation. This conformation is well established for transmembrane b cytochromes, but this appears to be the first example in a water-soluble cytochrome. The low-temperature m.c.d. spectra of the reduced form of the protein confirms that the haem contains a high-spin Fe2+ ligated by one His residue. The redox-linked spin-state change releases a His group. Since this residue is likely to bind a proton at pH values less than 6.5, this cytochrome may provide a useful model of a molecular mechanism of a redox-linked proton uptake and release process.</jats:p> |
| container_issue |
2 |
| container_start_page |
413 |
| container_title |
Biochemical Journal |
| container_volume |
270 |
| format_de105 |
Article, E-Article |
| format_de14 |
Article, E-Article |
| format_de15 |
Article, E-Article |
| format_de520 |
Article, E-Article |
| format_de540 |
Article, E-Article |
| format_dech1 |
Article, E-Article |
| format_ded117 |
Article, E-Article |
| format_degla1 |
E-Article |
| format_del152 |
Buch |
| format_del189 |
Article, E-Article |
| format_dezi4 |
Article |
| format_dezwi2 |
Article, E-Article |
| format_finc |
Article, E-Article |
| format_nrw |
Article, E-Article |
| _version_ |
1792339106766782475 |
| geogr_code |
not assigned |
| last_indexed |
2024-03-01T15:42:50.727Z |
| geogr_code_person |
not assigned |
| openURL |
url_ver=Z39.88-2004&ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fvufind.svn.sourceforge.net%3Agenerator&rft.title=Cytochrome+c%E2%80%B3+isolated+from+Methylophilus+methylotrophus.+An+example+of+bis-histidine-co-ordinated+Fe3%2B+haem%2C+with+near-perpendicular+orientation+of+the+ligands&rft.date=1990-09-01&genre=article&issn=1470-8728&volume=270&issue=2&spage=413&epage=417&pages=413-417&jtitle=Biochemical+Journal&atitle=Cytochrome+%3Ci%3Ec%3C%2Fi%3E%E2%80%B3+isolated+from+%3Ci%3EMethylophilus+methylotrophus%3C%2Fi%3E.+An+example+of+bis-histidine-co-ordinated+Fe3%2B+haem%2C+with+near-perpendicular+orientation+of+the+ligands&aulast=Turner&aufirst=D+L&rft_id=info%3Adoi%2F10.1042%2Fbj2700413&rft.language%5B0%5D=eng |
| SOLR | |
| _version_ | 1792339106766782475 |
| author | Berry, M J, George, S J, Thomson, A J, Santos, H, Turner, D L |
| author_facet | Berry, M J, George, S J, Thomson, A J, Santos, H, Turner, D L, Berry, M J, George, S J, Thomson, A J, Santos, H, Turner, D L |
| author_sort | berry, m j |
| container_issue | 2 |
| container_start_page | 413 |
| container_title | Biochemical Journal |
| container_volume | 270 |
| description | <jats:p>Cytochrome c″ (Methylophilus methylotrophus) is a soluble protein, Mr 15,000, possessing one haem which is high-spin in the reduced state but switches to a low-spin form on oxidation. Low-temperature electron-paramagnetic-resonance spectroscopy of the oxidized state shows a low-spin signal at gz = 3.65 with a folded line-shape typical of a haem of low rhombicity, and the near-infrared magnetic-circular-dichroism (m.c.d.) spectra reveal an unusually intense (delta epsilon = 400 M-1.cm-1 at 5 T, 4.2 K) charge-transfer band at 1560 nm, establishing that the oxidized haem is co-ordinated by two His residues in a near-perpendicular orientation. This conformation is well established for transmembrane b cytochromes, but this appears to be the first example in a water-soluble cytochrome. The low-temperature m.c.d. spectra of the reduced form of the protein confirms that the haem contains a high-spin Fe2+ ligated by one His residue. The redox-linked spin-state change releases a His group. Since this residue is likely to bind a proton at pH values less than 6.5, this cytochrome may provide a useful model of a molecular mechanism of a redox-linked proton uptake and release process.</jats:p> |
| doi_str_mv | 10.1042/bj2700413 |
| facet_avail | Online, Free |
| finc_class_facet | Chemie und Pharmazie, Biologie |
| format | ElectronicArticle |
| format_de105 | Article, E-Article |
| format_de14 | Article, E-Article |
| format_de15 | Article, E-Article |
| format_de520 | Article, E-Article |
| format_de540 | Article, E-Article |
| format_dech1 | Article, E-Article |
| format_ded117 | Article, E-Article |
| format_degla1 | E-Article |
| format_del152 | Buch |
| format_del189 | Article, E-Article |
| format_dezi4 | Article |
| format_dezwi2 | Article, E-Article |
| format_finc | Article, E-Article |
| format_nrw | Article, E-Article |
| geogr_code | not assigned |
| geogr_code_person | not assigned |
| id | ai-49-aHR0cDovL2R4LmRvaS5vcmcvMTAuMTA0Mi9iajI3MDA0MTM |
| imprint | Portland Press Ltd., 1990 |
| imprint_str_mv | Portland Press Ltd., 1990 |
| institution | DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161 |
| issn | 0264-6021, 1470-8728 |
| issn_str_mv | 0264-6021, 1470-8728 |
| language | English |
| last_indexed | 2024-03-01T15:42:50.727Z |
| match_str | berry1990cytochromecisolatedfrommethylophilusmethylotrophusanexampleofbishistidinecoordinatedfe3haemwithnearperpendicularorientationoftheligands |
| mega_collection | Portland Press Ltd. (CrossRef) |
| physical | 413-417 |
| publishDate | 1990 |
| publishDateSort | 1990 |
| publisher | Portland Press Ltd. |
| record_format | ai |
| recordtype | ai |
| series | Biochemical Journal |
| source_id | 49 |
| spelling | Berry, M J George, S J Thomson, A J Santos, H Turner, D L 0264-6021 1470-8728 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry http://dx.doi.org/10.1042/bj2700413 <jats:p>Cytochrome c″ (Methylophilus methylotrophus) is a soluble protein, Mr 15,000, possessing one haem which is high-spin in the reduced state but switches to a low-spin form on oxidation. Low-temperature electron-paramagnetic-resonance spectroscopy of the oxidized state shows a low-spin signal at gz = 3.65 with a folded line-shape typical of a haem of low rhombicity, and the near-infrared magnetic-circular-dichroism (m.c.d.) spectra reveal an unusually intense (delta epsilon = 400 M-1.cm-1 at 5 T, 4.2 K) charge-transfer band at 1560 nm, establishing that the oxidized haem is co-ordinated by two His residues in a near-perpendicular orientation. This conformation is well established for transmembrane b cytochromes, but this appears to be the first example in a water-soluble cytochrome. The low-temperature m.c.d. spectra of the reduced form of the protein confirms that the haem contains a high-spin Fe2+ ligated by one His residue. The redox-linked spin-state change releases a His group. Since this residue is likely to bind a proton at pH values less than 6.5, this cytochrome may provide a useful model of a molecular mechanism of a redox-linked proton uptake and release process.</jats:p> Cytochrome <i>c</i>″ isolated from <i>Methylophilus methylotrophus</i>. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands Biochemical Journal |
| spellingShingle | Berry, M J, George, S J, Thomson, A J, Santos, H, Turner, D L, Biochemical Journal, Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands, Cell Biology, Molecular Biology, Biochemistry |
| title | Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_full | Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_fullStr | Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_full_unstemmed | Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_short | Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| title_sort | cytochrome <i>c</i>″ isolated from <i>methylophilus methylotrophus</i>. an example of bis-histidine-co-ordinated fe3+ haem, with near-perpendicular orientation of the ligands |
| title_unstemmed | Cytochrome c″ isolated from Methylophilus methylotrophus. An example of bis-histidine-co-ordinated Fe3+ haem, with near-perpendicular orientation of the ligands |
| topic | Cell Biology, Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1042/bj2700413 |