@article{della_longa_dynamics_1992,
	title = {Dynamics of {CO} recombination in sperm whale myoglobin by dispersive {XANES}},
	volume = {258},
	issn = {0094-243X},
	url = {http://dx.doi.org/10.1063/1.42496},
	doi = {10.1063/1.42496},
	abstract = {The structural changes of the Fe active site following the low temperature photodissociation of sperm whale carboxymyoglobin (MbCO) has been studied by X‐ray Absorption Near Edge Structure (XANES) with the dispersive X‐ray absorption method. This experimental method allows to study time dependent biological processes in diluted samples in the time scale of 10–100 seconds. From the Fe K‐edge XANES difference spectra between the MbCO and its photoproduct (Mb*), a model of the intermediate state Mb* at low temperature (15 K) can be inferred. The structure of the photoproduct Mb* is non‐ligated, with the iron out of the heme plane, but distinct from the deoxy state Mb. A structural model built taking into account EXAFS and Raman data on Mb* explains some but not all the features observed by XANES spectroscopy. A smaller displacement of the iron from the pyrrolic nitrogen plane, coupled to a more domed structure of the porphyrin plane could explain better the spectral differences between the Mb* and Mb states.},
	number = {1},
	journal = {AIP Conf. Proc.},
	author = {Della Longa, S. and Bianconi, A. and Ascone, I. and Fontaine, A. and Congiu‐Castellano, A. and Borghini, G.},
	year = {1992},
	pages = {397--408}
}

{"_id":"rwwTC4b2K6Qqk58xD","bibbaseid":"dellalonga-bianconi-ascone-fontaine-congiucastellano-borghini-dynamicsofcorecombinationinspermwhalemyoglobinbydispersivexanes-1992","downloads":0,"creationDate":"2019-03-06T18:12:56.075Z","title":"Dynamics of CO recombination in sperm whale myoglobin by dispersive XANES","author_short":["Della Longa, S.","Bianconi, A.","Ascone, I.","Fontaine, A.","Congiu‐Castellano, A.","Borghini, G."],"year":1992,"bibtype":"article","biburl":"https://bibbase.org/zotero/abiancon","bibdata":{"bibtype":"article","type":"article","title":"Dynamics of CO recombination in sperm whale myoglobin by dispersive XANES","volume":"258","issn":"0094-243X","url":"http://dx.doi.org/10.1063/1.42496","doi":"10.1063/1.42496","abstract":"The structural changes of the Fe active site following the low temperature photodissociation of sperm whale carboxymyoglobin (MbCO) has been studied by X‐ray Absorption Near Edge Structure (XANES) with the dispersive X‐ray absorption method. This experimental method allows to study time dependent biological processes in diluted samples in the time scale of 10–100 seconds. From the Fe K‐edge XANES difference spectra between the MbCO and its photoproduct (Mb*), a model of the intermediate state Mb* at low temperature (15 K) can be inferred. The structure of the photoproduct Mb* is non‐ligated, with the iron out of the heme plane, but distinct from the deoxy state Mb. A structural model built taking into account EXAFS and Raman data on Mb* explains some but not all the features observed by XANES spectroscopy. A smaller displacement of the iron from the pyrrolic nitrogen plane, coupled to a more domed structure of the porphyrin plane could explain better the spectral differences between the Mb* and Mb states.","number":"1","journal":"AIP Conf. Proc.","author":[{"propositions":[],"lastnames":["Della","Longa"],"firstnames":["S."],"suffixes":[]},{"propositions":[],"lastnames":["Bianconi"],"firstnames":["A."],"suffixes":[]},{"propositions":[],"lastnames":["Ascone"],"firstnames":["I."],"suffixes":[]},{"propositions":[],"lastnames":["Fontaine"],"firstnames":["A."],"suffixes":[]},{"propositions":[],"lastnames":["Congiu‐Castellano"],"firstnames":["A."],"suffixes":[]},{"propositions":[],"lastnames":["Borghini"],"firstnames":["G."],"suffixes":[]}],"year":"1992","pages":"397–408","bibtex":"@article{della_longa_dynamics_1992,\n\ttitle = {Dynamics of {CO} recombination in sperm whale myoglobin by dispersive {XANES}},\n\tvolume = {258},\n\tissn = {0094-243X},\n\turl = {http://dx.doi.org/10.1063/1.42496},\n\tdoi = {10.1063/1.42496},\n\tabstract = {The structural changes of the Fe active site following the low temperature photodissociation of sperm whale carboxymyoglobin (MbCO) has been studied by X‐ray Absorption Near Edge Structure (XANES) with the dispersive X‐ray absorption method. This experimental method allows to study time dependent biological processes in diluted samples in the time scale of 10–100 seconds. From the Fe K‐edge XANES difference spectra between the MbCO and its photoproduct (Mb*), a model of the intermediate state Mb* at low temperature (15 K) can be inferred. The structure of the photoproduct Mb* is non‐ligated, with the iron out of the heme plane, but distinct from the deoxy state Mb. A structural model built taking into account EXAFS and Raman data on Mb* explains some but not all the features observed by XANES spectroscopy. A smaller displacement of the iron from the pyrrolic nitrogen plane, coupled to a more domed structure of the porphyrin plane could explain better the spectral differences between the Mb* and Mb states.},\n\tnumber = {1},\n\tjournal = {AIP Conf. Proc.},\n\tauthor = {Della Longa, S. and Bianconi, A. and Ascone, I. and Fontaine, A. and Congiu‐Castellano, A. and Borghini, G.},\n\tyear = {1992},\n\tpages = {397--408}\n}\n\n","author_short":["Della Longa, S.","Bianconi, A.","Ascone, I.","Fontaine, A.","Congiu‐Castellano, A.","Borghini, G."],"key":"della_longa_dynamics_1992","id":"della_longa_dynamics_1992","bibbaseid":"dellalonga-bianconi-ascone-fontaine-congiucastellano-borghini-dynamicsofcorecombinationinspermwhalemyoglobinbydispersivexanes-1992","role":"author","urls":{"Paper":"http://dx.doi.org/10.1063/1.42496"},"downloads":0},"search_terms":["dynamics","recombination","sperm","whale","myoglobin","dispersive","xanes","della longa","bianconi","ascone","fontaine","congiu‐castellano","borghini"],"keywords":[],"authorIDs":[],"dataSources":["qfSWh53k794ZuPrG9"]}