Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase
Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxid...
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| Veröffentlicht in: | Science (American Association for the Advancement of Science) 2014-07, Vol.345 (6193), p.193-197 |
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| creator | Casadei, Cecilia M. Gumiero, Andrea Metcalfe, Clive L. Murphy, Emma J. Basran, Jaswir Concilio, Maria Grazia Teixeira, Susana C. M. Schrader, Tobias E. Fielding, Alistair J. Ostermann, Andreas Blakeley, Matthew P. Raven, Emma L. Moody, Peter C. E. |
| description | Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; these allow direct visualization of protonation states. We demonstrate that the ferryl heme is an Fe(IV)=O species and is not protonated. Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O–O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates. |
| doi_str_mv | 10.1126/science.1254398 |
| format | Article |
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M. ; Schrader, Tobias E. ; Fielding, Alistair J. ; Ostermann, Andreas ; Blakeley, Matthew P. ; Raven, Emma L. ; Moody, Peter C. E.</creator><creatorcontrib>Casadei, Cecilia M. ; Gumiero, Andrea ; Metcalfe, Clive L. ; Murphy, Emma J. ; Basran, Jaswir ; Concilio, Maria Grazia ; Teixeira, Susana C. M. ; Schrader, Tobias E. ; Fielding, Alistair J. ; Ostermann, Andreas ; Blakeley, Matthew P. ; Raven, Emma L. ; Moody, Peter C. E.</creatorcontrib><description>Heme enzymes activate oxygen through formation of transient iron-oxo (ferryl) intermediates of the heme iron. A long-standing question has been the nature of the iron-oxygen bond and, in particular, the protonation state. We present neutron structures of the ferric derivative of cytochrome c peroxidase and its ferryl intermediate; these allow direct visualization of protonation states. We demonstrate that the ferryl heme is an Fe(IV)=O species and is not protonated. Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O–O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.1254398</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington: American Association for the Advancement of Science</publisher><subject>Atoms ; Biochemistry ; Crystallography ; Diffraction ; Enzymes ; Histidine ; Hydrogen ; Hydrogen bonds ; Iron ; Neutron scattering ; Neutrons ; Nuclear scattering ; Oxygen ; Peroxidase ; Protonation ; Protons ; Residues ; Scattering</subject><ispartof>Science (American Association for the Advancement of Science), 2014-07, Vol.345 (6193), p.193-197</ispartof><rights>Copyright © 2014 American Association for the Advancement of Science</rights><rights>Copyright © 2014, American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c468t-a7cde2333808a2d671128658f5be121b175597710f8d3ca25d1485b827d3473a3</citedby><cites>FETCH-LOGICAL-c468t-a7cde2333808a2d671128658f5be121b175597710f8d3ca25d1485b827d3473a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/24744975$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/24744975$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,777,781,800,2871,2872,27905,27906,57998,58231</link.rule.ids></links><search><creatorcontrib>Casadei, Cecilia M.</creatorcontrib><creatorcontrib>Gumiero, Andrea</creatorcontrib><creatorcontrib>Metcalfe, Clive L.</creatorcontrib><creatorcontrib>Murphy, Emma J.</creatorcontrib><creatorcontrib>Basran, Jaswir</creatorcontrib><creatorcontrib>Concilio, Maria Grazia</creatorcontrib><creatorcontrib>Teixeira, Susana C. 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Comparison of the structures shows that the distal histidine becomes protonated on formation of the ferryl intermediate, which has implications for the understanding of O–O bond cleavage in heme enzymes. The structures highlight the advantages of neutron cryo-crystallography in probing reaction mechanisms and visualizing protonation states in enzyme intermediates.</description><subject>Atoms</subject><subject>Biochemistry</subject><subject>Crystallography</subject><subject>Diffraction</subject><subject>Enzymes</subject><subject>Histidine</subject><subject>Hydrogen</subject><subject>Hydrogen bonds</subject><subject>Iron</subject><subject>Neutron scattering</subject><subject>Neutrons</subject><subject>Nuclear scattering</subject><subject>Oxygen</subject><subject>Peroxidase</subject><subject>Protonation</subject><subject>Protons</subject><subject>Residues</subject><subject>Scattering</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><recordid>eNpdkM1LxDAQxYMouK6ePQkBL17q5rNJj7L4BYte9OIlZNOp26Xb1CQF-98b2cWDDMwc5veGNw-hS0puKWXlIroWege3lEnBK32EZpRUsqgY4cdoRggvC02UPEVnMW4JybuKz9DHC4wp-B67MPkit5hs1_nPYIfNhJ0d0hgg4rQBPASffG9Tm-lMJcC-wQ2EMHV4AzvAbY8tHiD477a2Ec7RSWO7CBeHOUfvD_dvy6di9fr4vLxbFU6UOhVWuRoY51wTbVldqvyNLqVu5Booo2uqpKyUoqTRNXeWyZoKLdeaqZoLxS2fo5v93Wzwa4SYzK6NDrrO9uDHaGhFBMslaUav_6FbP4Y-uzNUihybYkxkarGnXPAxBmjMENqdDZOhxPxmbQ5Zm0PWWXG1V2xj8uEPZ0IJUSnJfwDsqXzP</recordid><startdate>20140711</startdate><enddate>20140711</enddate><creator>Casadei, Cecilia M.</creator><creator>Gumiero, Andrea</creator><creator>Metcalfe, Clive L.</creator><creator>Murphy, Emma J.</creator><creator>Basran, Jaswir</creator><creator>Concilio, Maria Grazia</creator><creator>Teixeira, Susana C. 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| ispartof | Science (American Association for the Advancement of Science), 2014-07, Vol.345 (6193), p.193-197 |
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| source | American Association for the Advancement of Science; Jstor Complete Legacy |
| subjects | Atoms Biochemistry Crystallography Diffraction Enzymes Histidine Hydrogen Hydrogen bonds Iron Neutron scattering Neutrons Nuclear scattering Oxygen Peroxidase Protonation Protons Residues Scattering |
| title | Neutron cryo-crystallography captures the protonation state of ferryl heme in a peroxidase |
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