Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin
Peroxide- induced oxidative modi. cations of haem proteins such as myoglobin and haemoglobin can lead to the formation of a covalent bond between the haem and globin. These haem to protein cross- linked forms of myoglobin and haemoglobin are cytotoxic and have been identified in pathological conditi...
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TAYLOR & FRANCIS INC
2007
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Online Access: | http://hdl.handle.net/11573/47541 https://doi.org/10.1080/15216540601178083 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000248721400002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-34547948951&partnerID=65&md5=0b3b97eabe7355adee37ec62e637061b |
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ftunivromairis:oai:iris.uniroma1.it:11573/47541 2024-02-27T08:45:41+00:00 Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin Brandon J. Reeder Maria Giulia Bigotti Nicholas J. Watmough Michael T. Wilson CUTRUZZOLA', Francesca Brandon J., Reeder Cutruzzola', Francesca Maria Giulia, Bigotti Nicholas J., Watmough Michael T., Wilson 2007 http://hdl.handle.net/11573/47541 https://doi.org/10.1080/15216540601178083 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000248721400002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-34547948951&partnerID=65&md5=0b3b97eabe7355adee37ec62e637061b eng eng TAYLOR & FRANCIS INC info:eu-repo/semantics/altIdentifier/pmid/17701542 info:eu-repo/semantics/altIdentifier/wos/WOS:000248721400002 volume:59 issue:8-9 firstpage:477 lastpage:489 numberofpages:13 journal:IUBMB LIFE http://hdl.handle.net/11573/47541 doi:10.1080/15216540601178083 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34547948951 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000248721400002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-34547948951&partnerID=65&md5=0b3b97eabe7355adee37ec62e637061b aplysia ferryl histidine myoglobin peroxide tyrosine info:eu-repo/semantics/article 2007 ftunivromairis https://doi.org/10.1080/15216540601178083 2024-01-31T18:07:39Z Peroxide- induced oxidative modi. cations of haem proteins such as myoglobin and haemoglobin can lead to the formation of a covalent bond between the haem and globin. These haem to protein cross- linked forms of myoglobin and haemoglobin are cytotoxic and have been identified in pathological conditions in vivo. An understanding of the mechanism of haem to protein cross- link formation could provide important information on the mechanisms of the oxidative processes that lead to pathological complications associated with the formation of these altered myoglobins and haemoglobins. We have re- examined the mechanism of the formation of haem to protein cross- link to test the previously reported hypothesis that the haem forms a covalent bond to the protein via the tyrosine 103 residue ( Catalano, C. E., Choe, Y. S., Ortiz de Montellano, P. R., J. Biol. Chem. 1989, 10534 - 10541). Comparison of native horse myoglobin, recombinant sperm whale myoglobin and Tyr 103 -> Phe sperm whale mutant shows that, contrary to the previously proposed mechanism of haem to protein cross- link formation, the absence of tyrosine 103 has no impact on the formation of haem to protein cross- links. In contrast, we have found that engineered myoglobins that lack the distal histidine residue either cannot generate haem to protein cross- links or show greatly suppressed levels of modified protein. Moreover, addition of a distal histidine to myoglobin from Aplysia limacina, that naturally lacks this histidine, restores the haem protein's capacity to generate haem to protein cross- links. The distal histidine is, therefore, vital for the formation of haem to protein cross- link and we explore this outcome. Article in Journal/Newspaper Sperm whale Sapienza Università di Roma: CINECA IRIS Ortiz ENVELOPE(-59.717,-59.717,-62.450,-62.450) IUBMB Life 59 8 477 489 |
institution |
Open Polar |
collection |
Sapienza Università di Roma: CINECA IRIS |
op_collection_id |
ftunivromairis |
language |
English |
topic |
aplysia ferryl histidine myoglobin peroxide tyrosine |
spellingShingle |
aplysia ferryl histidine myoglobin peroxide tyrosine Brandon J. Reeder Maria Giulia Bigotti Nicholas J. Watmough Michael T. Wilson CUTRUZZOLA', Francesca Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin |
topic_facet |
aplysia ferryl histidine myoglobin peroxide tyrosine |
description |
Peroxide- induced oxidative modi. cations of haem proteins such as myoglobin and haemoglobin can lead to the formation of a covalent bond between the haem and globin. These haem to protein cross- linked forms of myoglobin and haemoglobin are cytotoxic and have been identified in pathological conditions in vivo. An understanding of the mechanism of haem to protein cross- link formation could provide important information on the mechanisms of the oxidative processes that lead to pathological complications associated with the formation of these altered myoglobins and haemoglobins. We have re- examined the mechanism of the formation of haem to protein cross- link to test the previously reported hypothesis that the haem forms a covalent bond to the protein via the tyrosine 103 residue ( Catalano, C. E., Choe, Y. S., Ortiz de Montellano, P. R., J. Biol. Chem. 1989, 10534 - 10541). Comparison of native horse myoglobin, recombinant sperm whale myoglobin and Tyr 103 -> Phe sperm whale mutant shows that, contrary to the previously proposed mechanism of haem to protein cross- link formation, the absence of tyrosine 103 has no impact on the formation of haem to protein cross- links. In contrast, we have found that engineered myoglobins that lack the distal histidine residue either cannot generate haem to protein cross- links or show greatly suppressed levels of modified protein. Moreover, addition of a distal histidine to myoglobin from Aplysia limacina, that naturally lacks this histidine, restores the haem protein's capacity to generate haem to protein cross- links. The distal histidine is, therefore, vital for the formation of haem to protein cross- link and we explore this outcome. |
author2 |
Brandon J., Reeder Cutruzzola', Francesca Maria Giulia, Bigotti Nicholas J., Watmough Michael T., Wilson |
format |
Article in Journal/Newspaper |
author |
Brandon J. Reeder Maria Giulia Bigotti Nicholas J. Watmough Michael T. Wilson CUTRUZZOLA', Francesca |
author_facet |
Brandon J. Reeder Maria Giulia Bigotti Nicholas J. Watmough Michael T. Wilson CUTRUZZOLA', Francesca |
author_sort |
Brandon J. Reeder |
title |
Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin |
title_short |
Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin |
title_full |
Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin |
title_fullStr |
Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin |
title_full_unstemmed |
Histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin |
title_sort |
histidine and not tyrosine is required for the peroxide-induced formation of haem to protein cross-linked myoglobin |
publisher |
TAYLOR & FRANCIS INC |
publishDate |
2007 |
url |
http://hdl.handle.net/11573/47541 https://doi.org/10.1080/15216540601178083 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000248721400002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-34547948951&partnerID=65&md5=0b3b97eabe7355adee37ec62e637061b |
long_lat |
ENVELOPE(-59.717,-59.717,-62.450,-62.450) |
geographic |
Ortiz |
geographic_facet |
Ortiz |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
info:eu-repo/semantics/altIdentifier/pmid/17701542 info:eu-repo/semantics/altIdentifier/wos/WOS:000248721400002 volume:59 issue:8-9 firstpage:477 lastpage:489 numberofpages:13 journal:IUBMB LIFE http://hdl.handle.net/11573/47541 doi:10.1080/15216540601178083 info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-34547948951 http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=000248721400002&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=0c7ff228ccbaaa74236f48834a34396a http://www.scopus.com/inward/record.url?eid=2-s2.0-34547948951&partnerID=65&md5=0b3b97eabe7355adee37ec62e637061b |
op_doi |
https://doi.org/10.1080/15216540601178083 |
container_title |
IUBMB Life |
container_volume |
59 |
container_issue |
8 |
container_start_page |
477 |
op_container_end_page |
489 |
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1792054981755404288 |