Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)).
The time course of ligand recombination to the myoglobin from Aplysia limacina, which has Val(E7), was measured following photolysis by flashes of 35 ps to 300 ns with a time resolution of 10 ps or 1 ns. CO shows only biomolecular recombination. O2 has a small geminate reaction with a half-time of t...
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1990
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Online Access: | https://www.openaccessrepository.it/record/89509 https://doi.org/10.1016/s0021-9258(18)77390-0 |
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ftopenaccessrep:oai:zenodo.org:89509 2023-10-25T01:44:08+02:00 Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)). R S Blackmore Q H Gibson Andrea Bellelli 1990-08-15 https://www.openaccessrepository.it/record/89509 https://doi.org/10.1016/s0021-9258(18)77390-0 eng eng url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/89509 doi:10.1016/s0021-9258(18)77390-0 info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ Cell Biology Molecular Biology Biochemistry info:eu-repo/semantics/article publication-article 1990 ftopenaccessrep https://doi.org/10.1016/s0021-9258(18)77390-0 2023-09-26T22:19:16Z The time course of ligand recombination to the myoglobin from Aplysia limacina, which has Val(E7), was measured following photolysis by flashes of 35 ps to 300 ns with a time resolution of 10 ps or 1 ns. CO shows only biomolecular recombination. O2 has a small geminate reaction with a half-time of tens of picoseconds, but no nanosecond geminate reaction. NO has two picosecond relaxations with half-times of 70 ps (15%) and 1 ns (80%) and one nanosecond relaxation with a half-time of 4.6 ns. The biomolecular rates for O2 and NO are the same: 2 x 10(7) M-1 s-1. Methyl and ethyl isonitriles have a geminate reaction with a half-time of 35 ps. Ethyl isonitrile has, in addition, a nanosecond relaxation (25%) with a half-time of 100 ns. t-Butyl isonitrile has four geminate relaxations (10 ps, 35 ps, 1 ns, and 1 microseconds). Analysis of the results suggests much easier movement of ligand between the heme pocket and the exterior than in sperm whale myoglobin (His(E7]. The reactivity of the heme is little different, placing the effect of the differences from sperm whale myoglobin on the distal side of the heme. Article in Journal/Newspaper Sperm whale Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository Journal of Biological Chemistry 265 23 13595 13600 |
institution |
Open Polar |
collection |
Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository |
op_collection_id |
ftopenaccessrep |
language |
English |
topic |
Cell Biology Molecular Biology Biochemistry |
spellingShingle |
Cell Biology Molecular Biology Biochemistry R S Blackmore Q H Gibson Andrea Bellelli Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)). |
topic_facet |
Cell Biology Molecular Biology Biochemistry |
description |
The time course of ligand recombination to the myoglobin from Aplysia limacina, which has Val(E7), was measured following photolysis by flashes of 35 ps to 300 ns with a time resolution of 10 ps or 1 ns. CO shows only biomolecular recombination. O2 has a small geminate reaction with a half-time of tens of picoseconds, but no nanosecond geminate reaction. NO has two picosecond relaxations with half-times of 70 ps (15%) and 1 ns (80%) and one nanosecond relaxation with a half-time of 4.6 ns. The biomolecular rates for O2 and NO are the same: 2 x 10(7) M-1 s-1. Methyl and ethyl isonitriles have a geminate reaction with a half-time of 35 ps. Ethyl isonitrile has, in addition, a nanosecond relaxation (25%) with a half-time of 100 ns. t-Butyl isonitrile has four geminate relaxations (10 ps, 35 ps, 1 ns, and 1 microseconds). Analysis of the results suggests much easier movement of ligand between the heme pocket and the exterior than in sperm whale myoglobin (His(E7]. The reactivity of the heme is little different, placing the effect of the differences from sperm whale myoglobin on the distal side of the heme. |
format |
Article in Journal/Newspaper |
author |
R S Blackmore Q H Gibson Andrea Bellelli |
author_facet |
R S Blackmore Q H Gibson Andrea Bellelli |
author_sort |
R S Blackmore |
title |
Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)). |
title_short |
Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)). |
title_full |
Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)). |
title_fullStr |
Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)). |
title_full_unstemmed |
Ligand binding to a hemoprotein lacking the distal histidine. The myoglobin from aplysia limacina (Val(E7)). |
title_sort |
ligand binding to a hemoprotein lacking the distal histidine. the myoglobin from aplysia limacina (val(e7)). |
publishDate |
1990 |
url |
https://www.openaccessrepository.it/record/89509 https://doi.org/10.1016/s0021-9258(18)77390-0 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/89509 doi:10.1016/s0021-9258(18)77390-0 |
op_rights |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by/4.0/ |
op_doi |
https://doi.org/10.1016/s0021-9258(18)77390-0 |
container_title |
Journal of Biological Chemistry |
container_volume |
265 |
container_issue |
23 |
container_start_page |
13595 |
op_container_end_page |
13600 |
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1780741519238496256 |