A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR
The solution H-1 NMR structure of the active site and ligand dissociation rate for the cyanomet complex have been determined for a sperm whale myoglobin triple mutant Leu29(B10) --> Tyr, His64(E7) --> Gln, Thr67(E10) --> Arg that mimics the distal residue configuration of the oxygen-avid he...
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BIOPHYSICAL SOCIETY, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3998
1997
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Online Access: | http://hdl.handle.net/11573/406452 https://doi.org/10.1016/S0006-34 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1997XM53700043&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0030749504&partnerID=65&md5=8a623a4c155f7a477f09bd92b2b93b3c |
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ftunivromairis:oai:iris.uniroma1.it:11573/406452 2024-02-27T08:45:42+00:00 A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR Zhang W LaMar GN CUTRUZZOLA', Francesca TRAVAGLINI ALLOCATELLI, Carlo BRUNORI, Maurizio Zhang, W Cutruzzola', Francesca TRAVAGLINI ALLOCATELLI, Carlo Brunori, Maurizio Lamar, Gn 1997 http://hdl.handle.net/11573/406452 https://doi.org/10.1016/S0006-34 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1997XM53700043&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0030749504&partnerID=65&md5=8a623a4c155f7a477f09bd92b2b93b3c eng eng BIOPHYSICAL SOCIETY, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3998 info:eu-repo/semantics/altIdentifier/pmid/9251819 info:eu-repo/semantics/altIdentifier/wos/WOS:A1997XM53700043 volume:73 issue:2 firstpage:1019 lastpage:1030 numberofpages:12 journal:BIOPHYSICAL JOURNAL http://hdl.handle.net/11573/406452 doi:10.1016/S0006-34 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0030749504 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1997XM53700043&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0030749504&partnerID=65&md5=8a623a4c155f7a477f09bd92b2b93b3c info:eu-repo/semantics/article 1997 ftunivromairis https://doi.org/10.1016/S0006-34 2024-01-31T18:08:08Z The solution H-1 NMR structure of the active site and ligand dissociation rate for the cyanomet complex have been determined for a sperm whale myoglobin triple mutant Leu29(B10) --> Tyr, His64(E7) --> Gln, Thr67(E10) --> Arg that mimics the distal residue configuration of the oxygen-avid hemoglobin from Ascaris suum. A double mutant that retains Leu29(B10) was similarly investigated. Two-dimensional NMR analysis of the iron-induced dipolar shifts, together with the conserved proximal side structure for the two mutants, allowed the determination of the orientations of the Paramagnetic susceptibility tensor for each complex. The resulting magnetic axes, together with paramagnetic relaxation and steady-state NOEs, led to a quantitative description of the distal residue orientations. The distal Tyr29(B10) in the triple mutant provides a strong hydrogen bond to the bound cyanide comparable to that provided by His64(E7) in wild-type myoglobin. The distal Gln64(E7) in the triple mutant is sufficiently close to the bound cyanide to serve as a hydrogen bond donor, but the angle is not consistent with a strong hydrogen bond. Dipolar contacts between the Arg67(E10) guanidinium group and the Gln64(E7) side chain in both mutants support a hydrogen-bond to the Gln64(E7) carbonyl group. The much lower oxygen affinity of this triple mutant relative to that of Ascaris hemoglobin is concluded to arise from side-chain orientations that do not allow hydrogen bonds between the Gln64(E7) side-chain NHs and both the ligand and Tyr29(B10) hydroxyl oxygen. Cyanide dissociation rates for the reduced cyanide complexes are virtually unaffected by the mutations and are consistent with a model of the rate-determining step as the intrinsically slow Fe-C bond breaking that is largely independent of any hydrogen bonds to the cyanide nitrogen. Article in Journal/Newspaper Sperm whale Sapienza Università di Roma: CINECA IRIS |
institution |
Open Polar |
collection |
Sapienza Università di Roma: CINECA IRIS |
op_collection_id |
ftunivromairis |
language |
English |
description |
The solution H-1 NMR structure of the active site and ligand dissociation rate for the cyanomet complex have been determined for a sperm whale myoglobin triple mutant Leu29(B10) --> Tyr, His64(E7) --> Gln, Thr67(E10) --> Arg that mimics the distal residue configuration of the oxygen-avid hemoglobin from Ascaris suum. A double mutant that retains Leu29(B10) was similarly investigated. Two-dimensional NMR analysis of the iron-induced dipolar shifts, together with the conserved proximal side structure for the two mutants, allowed the determination of the orientations of the Paramagnetic susceptibility tensor for each complex. The resulting magnetic axes, together with paramagnetic relaxation and steady-state NOEs, led to a quantitative description of the distal residue orientations. The distal Tyr29(B10) in the triple mutant provides a strong hydrogen bond to the bound cyanide comparable to that provided by His64(E7) in wild-type myoglobin. The distal Gln64(E7) in the triple mutant is sufficiently close to the bound cyanide to serve as a hydrogen bond donor, but the angle is not consistent with a strong hydrogen bond. Dipolar contacts between the Arg67(E10) guanidinium group and the Gln64(E7) side chain in both mutants support a hydrogen-bond to the Gln64(E7) carbonyl group. The much lower oxygen affinity of this triple mutant relative to that of Ascaris hemoglobin is concluded to arise from side-chain orientations that do not allow hydrogen bonds between the Gln64(E7) side-chain NHs and both the ligand and Tyr29(B10) hydroxyl oxygen. Cyanide dissociation rates for the reduced cyanide complexes are virtually unaffected by the mutations and are consistent with a model of the rate-determining step as the intrinsically slow Fe-C bond breaking that is largely independent of any hydrogen bonds to the cyanide nitrogen. |
author2 |
Zhang, W Cutruzzola', Francesca TRAVAGLINI ALLOCATELLI, Carlo Brunori, Maurizio Lamar, Gn |
format |
Article in Journal/Newspaper |
author |
Zhang W LaMar GN CUTRUZZOLA', Francesca TRAVAGLINI ALLOCATELLI, Carlo BRUNORI, Maurizio |
spellingShingle |
Zhang W LaMar GN CUTRUZZOLA', Francesca TRAVAGLINI ALLOCATELLI, Carlo BRUNORI, Maurizio A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR |
author_facet |
Zhang W LaMar GN CUTRUZZOLA', Francesca TRAVAGLINI ALLOCATELLI, Carlo BRUNORI, Maurizio |
author_sort |
Zhang W |
title |
A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR |
title_short |
A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR |
title_full |
A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR |
title_fullStr |
A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR |
title_full_unstemmed |
A myoglobin mutant designed to mimic the oxygen-avid Ascaris suum hemoglobin: Elucidation of the distal hydrogen bonding network by solution NMR |
title_sort |
myoglobin mutant designed to mimic the oxygen-avid ascaris suum hemoglobin: elucidation of the distal hydrogen bonding network by solution nmr |
publisher |
BIOPHYSICAL SOCIETY, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3998 |
publishDate |
1997 |
url |
http://hdl.handle.net/11573/406452 https://doi.org/10.1016/S0006-34 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1997XM53700043&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0030749504&partnerID=65&md5=8a623a4c155f7a477f09bd92b2b93b3c |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/9251819 info:eu-repo/semantics/altIdentifier/wos/WOS:A1997XM53700043 volume:73 issue:2 firstpage:1019 lastpage:1030 numberofpages:12 journal:BIOPHYSICAL JOURNAL http://hdl.handle.net/11573/406452 doi:10.1016/S0006-34 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0030749504 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=A1997XM53700043&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-0030749504&partnerID=65&md5=8a623a4c155f7a477f09bd92b2b93b3c |
op_doi |
https://doi.org/10.1016/S0006-34 |
_version_ |
1792054992037740544 |