A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue
The homodimeric hemoglobin (HbN) from Mycobacterium tuberculosis displays an extremely high oxygen binding affinity and cooperativity. Sequence alignment with other hemoglobins suggests that the proximal F8 ligand is histidine, the distal E7 residue is leucine, and the B10 position is occupied by ty...
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| Veröffentlicht in: | The Journal of biological chemistry 2000-01, Vol.275 (3), p.1679-1684 |
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| container_title | The Journal of biological chemistry |
| container_volume | 275 |
| creator | Yeh, S R Couture, M Ouellet, Y Guertin, M Rousseau, D L |
| description | The homodimeric hemoglobin (HbN) from Mycobacterium tuberculosis displays an extremely high oxygen binding affinity and cooperativity. Sequence alignment with other hemoglobins suggests that the proximal F8 ligand is histidine, the distal E7 residue is leucine, and the B10 position is occupied by tyrosine. To determine how these heme pocket residues regulate the ligand binding affinities and physiological functions of HbN, we have measured the resonance Raman spectra of the O(2), CO, and OH(-) derivatives of the wild type protein and the B10 Tyr --> Leu and Phe mutants. Taken together these data demonstrate a unique distal environment in which the heme bound ligands strongly interact with the B10 tyrosine residue. The implications of these data on the physiological functions of HbN and another heme-containing protein, cytochrome c oxidase, are considered. |
| doi_str_mv | 10.1074/jbc.275.3.1679 |
| format | Article |
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Taken together these data demonstrate a unique distal environment in which the heme bound ligands strongly interact with the B10 tyrosine residue. 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The implications of these data on the physiological functions of HbN and another heme-containing protein, cytochrome c oxidase, are considered.</description><subject>Carbon Monoxide - chemistry</subject><subject>Heme - chemistry</subject><subject>Hemoglobins - chemistry</subject><subject>Hydrogen - chemistry</subject><subject>Hydroxides - chemistry</subject><subject>Ligands</subject><subject>Models, Chemical</subject><subject>Mycobacterium tuberculosis</subject><subject>Mycobacterium tuberculosis - chemistry</subject><subject>Oxygen - chemistry</subject><subject>Recombinant Proteins - chemistry</subject><subject>Spectrum Analysis, Raman</subject><subject>Tyrosine - chemistry</subject><issn>0021-9258</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kL1PwzAQxT2AaCmsjMgTW4Idx04yVhVfUhEDMEe2cw6unLjYCSKs_OMEUW55Or3fe9IdQheUpJQU-fVO6TQreMpSKorqCC0JyWhSZbxcoNMYd2SevKInaEGJYKIU2RJ9r7H2fg9BDvYDsP-cWuixsn1j-xa_Qedb5-cVm-A7_Dhpr6QeINixw8OoIOjR-Whjip8HqayzX3OR77E3v2HAzraybyJWE5a4sXGQDg9TmCM94ADRNiOcoWMjXYTzg67Q6-3Ny-Y-2T7dPWzW22RPORsSpbQ2DTOKk6JkjdFMU1M1803cUJC8yjNp8nw2RQXClEoyELwsBdEF05qzFbr6690H_z5CHOrORg3OyR78GGta5EIQUszg5QEcVQdNvQ-2k2Gq_9_GfgCPEXD8</recordid><startdate>20000121</startdate><enddate>20000121</enddate><creator>Yeh, S R</creator><creator>Couture, M</creator><creator>Ouellet, Y</creator><creator>Guertin, M</creator><creator>Rousseau, D L</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope></search><sort><creationdate>20000121</creationdate><title>A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. 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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Carbon Monoxide - chemistry Heme - chemistry Hemoglobins - chemistry Hydrogen - chemistry Hydroxides - chemistry Ligands Models, Chemical Mycobacterium tuberculosis Mycobacterium tuberculosis - chemistry Oxygen - chemistry Recombinant Proteins - chemistry Spectrum Analysis, Raman Tyrosine - chemistry |
| title | A cooperative oxygen binding hemoglobin from Mycobacterium tuberculosis. Stabilization of heme ligands by a distal tyrosine residue |
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