Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state
The photodissociation and geminate recombination of nitric oxide in myoglobin, under continuous illumination, is modeled computationally. The relaxation of the photon energy into the protein matrix is also considered in a single simulation scheme that mimics a complete experimental setup. The dynami...
Published in: | The Journal of Physical Chemistry B |
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AMER CHEMICAL SOC
2012
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Online Access: | http://hdl.handle.net/11573/463896 https://doi.org/10.1021/jp212148x http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000301509500037&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-84858309807&partnerID=65&md5=7cd86c8a3bc7f42d3080b08704204991 |
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ftunivromairis:oai:iris.uniroma1.it:11573/463896 2024-02-27T08:45:42+00:00 Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state Grazia Cottone Gianluca Lattanzi Ron Elber CICCOTTI, Giovanni Grazia, Cottone Gianluca, Lattanzi Ciccotti, Giovanni Ron, Elber 2012 STAMPA http://hdl.handle.net/11573/463896 https://doi.org/10.1021/jp212148x http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000301509500037&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-84858309807&partnerID=65&md5=7cd86c8a3bc7f42d3080b08704204991 eng eng AMER CHEMICAL SOC info:eu-repo/semantics/altIdentifier/pmid/22356468 info:eu-repo/semantics/altIdentifier/wos/WOS:000301509500037 volume:116 issue:10 firstpage:3397 lastpage:3410 numberofpages:14 journal:JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL http://hdl.handle.net/11573/463896 doi:10.1021/jp212148x info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84858309807 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000301509500037&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-84858309807&partnerID=65&md5=7cd86c8a3bc7f42d3080b08704204991 info:eu-repo/semantics/article 2012 ftunivromairis https://doi.org/10.1021/jp212148x 2024-01-31T18:08:03Z The photodissociation and geminate recombination of nitric oxide in myoglobin, under continuous illumination, is modeled computationally. The relaxation of the photon energy into the protein matrix is also considered in a single simulation scheme that mimics a complete experimental setup. The dynamic approach to non-equilibrium molecular dynamics is used, starting from a steady state, to compute its relaxation to equilibrium. Simulations are conducted for the native form of sperm whale myoglobin and for two other mutants, V68W and L29F, illustrating a fair diversity of spatial and temporal geminate recombination processes. Energy flow to the heme and immediate protein environment provide hints to allostery. In particular, a pathway of energy flow between the heme and the FG loop is illustrated. Although the simulations were conducted for myoglobin only, the thermal fluctuations of the FG corner are in agreement with the large structural shifts of FG during the allosteric transition of tetrameric hemoglobin. © 2012 American Chemical Society. Article in Journal/Newspaper Sperm whale Sapienza Università di Roma: CINECA IRIS The Journal of Physical Chemistry B 116 10 3397 3410 |
institution |
Open Polar |
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Sapienza Università di Roma: CINECA IRIS |
op_collection_id |
ftunivromairis |
language |
English |
description |
The photodissociation and geminate recombination of nitric oxide in myoglobin, under continuous illumination, is modeled computationally. The relaxation of the photon energy into the protein matrix is also considered in a single simulation scheme that mimics a complete experimental setup. The dynamic approach to non-equilibrium molecular dynamics is used, starting from a steady state, to compute its relaxation to equilibrium. Simulations are conducted for the native form of sperm whale myoglobin and for two other mutants, V68W and L29F, illustrating a fair diversity of spatial and temporal geminate recombination processes. Energy flow to the heme and immediate protein environment provide hints to allostery. In particular, a pathway of energy flow between the heme and the FG loop is illustrated. Although the simulations were conducted for myoglobin only, the thermal fluctuations of the FG corner are in agreement with the large structural shifts of FG during the allosteric transition of tetrameric hemoglobin. © 2012 American Chemical Society. |
author2 |
Grazia, Cottone Gianluca, Lattanzi Ciccotti, Giovanni Ron, Elber |
format |
Article in Journal/Newspaper |
author |
Grazia Cottone Gianluca Lattanzi Ron Elber CICCOTTI, Giovanni |
spellingShingle |
Grazia Cottone Gianluca Lattanzi Ron Elber CICCOTTI, Giovanni Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state |
author_facet |
Grazia Cottone Gianluca Lattanzi Ron Elber CICCOTTI, Giovanni |
author_sort |
Grazia Cottone |
title |
Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state |
title_short |
Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state |
title_full |
Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state |
title_fullStr |
Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state |
title_full_unstemmed |
Multiphoton absorption of myoglobin-nitric oxide complex: Relaxation by D-NEMD of a stationary state |
title_sort |
multiphoton absorption of myoglobin-nitric oxide complex: relaxation by d-nemd of a stationary state |
publisher |
AMER CHEMICAL SOC |
publishDate |
2012 |
url |
http://hdl.handle.net/11573/463896 https://doi.org/10.1021/jp212148x http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000301509500037&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-84858309807&partnerID=65&md5=7cd86c8a3bc7f42d3080b08704204991 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/22356468 info:eu-repo/semantics/altIdentifier/wos/WOS:000301509500037 volume:116 issue:10 firstpage:3397 lastpage:3410 numberofpages:14 journal:JOURNAL OF PHYSICAL CHEMISTRY. B, CONDENSED MATTER, MATERIALS, SURFACES, INTERFACES & BIOPHYSICAL http://hdl.handle.net/11573/463896 doi:10.1021/jp212148x info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84858309807 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000301509500037&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-84858309807&partnerID=65&md5=7cd86c8a3bc7f42d3080b08704204991 |
op_doi |
https://doi.org/10.1021/jp212148x |
container_title |
The Journal of Physical Chemistry B |
container_volume |
116 |
container_issue |
10 |
container_start_page |
3397 |
op_container_end_page |
3410 |
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1792054985264988160 |