{"refrec":{"BRefID":280976,"RR":"<b>Pesce, A.; Nardini, M.; Ascenzi, P.; Geuens, E.; Dewilde, S.; Moens, L.; Bolognesi, M.; Riggs, A.F.; Hale, A.; Deng, P.; Nienhaus, G.U.; Olson, J.S.; Nienhaus, K.</b> (2004). Thr-E11 regulates O-2 affinity in <i>Cerebratulus lacteus</i> mini-hemoglobin. <i>J. Biol. Chem. 279(32)</i>: 33662-33672. <a href=\"https://dx.doi.org/10.1074/jbc.M403597200\" target=\"_blank\">https://dx.doi.org/10.1074/jbc.M403597200</a>","BEntID":272995,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":1,"RefStringPartII":". <i>J. Biol. Chem. 279(32)</i>: 33662-33672. <a href=\"https://dx.doi.org/10.1074/jbc.M403597200\" target=\"_blank\">https://dx.doi.org/10.1074/jbc.M403597200</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Pesce, A.; Nardini, M.; Ascenzi, P.; Geuens, E.; Dewilde, S.; Moens, L.; Bolognesi, M.; Riggs, A.F.; Hale, A.; Deng, P.; Nienhaus, G.U.; Olson, J.S.; Nienhaus, K.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Pesce, A. <i>et al.</i>","Englishabstract":"The mini-hemoglobin from <i>Cerebratulus lacteus</i> (CerHb) belongs to a class of globins containing the polar Tyr-B10/Gln-E7 amino acid pair that normally causes low rates of O<sub>2</sub> dissociation and ultra-high O<sub>2</sub> affinity, which suggest O<sub>2</sub> sensing or NO scavenging functions. CerHb, however, has high rates of O<sub>2</sub> dissociation (<i>k</i><sub>O2</sub> = 200-600 s<sup>-1</sup>) and moderate O<sub>2</sub> affinity (<i>K</i><sub>O2</sub> ≈1 μm<sup>-1</sup>) as a result of a third polar amino acid in its active site, Thr-E11. When Thr-E11 is replaced by Val, <i>k</i><sub>O2</sub> decreases 1000-fold and <i>K</i><sub>O2</sub> increases 130-fold at pH 7.0, 20 °C. The mutation also shifts the stretching frequencies of both heme-bound and photodissociated CO, indicating marked changes of the electrostatic field at the active site. The crystal structure of Thr-E11 → Val CerHbO<sub>2</sub> at 1.70 Å resolution is almost identical to that of the wild-type protein (root mean square deviation of 0.12 Å). The dramatic functional and spectral effects of the Thr-E11 → Val mutation are due exclusively to changes in the hydrogen bonding network in the active site. Replacing Thr-E11 with Val “frees” the Tyr-B10 hydroxyl group to rotate toward and donate a strong hydrogen bond to the heme-bound ligand, causing a selective increase in O<sub>2</sub> affinity, a decrease of the rate coefficient for O<sub>2</sub> dissociation, a 40 cm<sup>-1</sup> decrease in ν<sub>CO</sub> of heme-bound CO, and an increase in ligand migration toward more remote intermediate sites.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Thr-E11 regulates O-2 affinity in <i>Cerebratulus lacteus</i> mini-hemoglobin","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-23 01:32:42.490680","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":null,"OtherDescriptors":null,"Notes":null,"AnaPub":2004,"MonPub":null,"DateUpdate":"2022-07-14","DateCreate":"2016-10-09","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000223039700076","VABBcode":null,"OpenAcc":0,"DOI":"10.1074/jbc.M403597200"},"refs":null,"anarec":{"AnaID":280976,"PubliDate":2004,"Pagination":"33662-33672","XtraPublOfAnaID":null,"ISBN":null,"Volume":"279","Issue":"32","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":43206,"SerRR":"Journal of Biological Chemistry. 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