Bacellar, CamilaKinschel, DominikCannelli, OlivieroSorokin, BorisKatayama, TetsuoMancini, Giulia F.Rouxel, Jeremy R.Obara, YukiNishitani, JunichiIto, HironoriIto, TerumasaKurahashi, NaoyaHigashimura, ChikaKudo, ShotaroCirelli, ClaudioKnopp, GregorNass, KarolJohnson, Philip J. M.Wach, AnnaSzlachetko, JakubLima, Frederico A.Milne, Christopher J.Yabashi, MakinaSuzuki, ToshinoriMisawa, KazuhikoChergui, Majed2021-09-112021-09-112021-09-112021-05-0110.1039/d0fd00131ghttps://infoscience.epfl.ch/handle/20.500.14299/181369WOS:000664793300015We discuss our recently reported femtosecond (fs) X-ray emission spectroscopy results on the ligand dissociation and recombination in nitrosylmyoglobin (MbNO) in the context of previous studies on ferrous haem proteins. We also present a preliminary account of femtosecond X-ray absorption studies on MbNO, pointing to the presence of more than one species formed upon photolysis.Chemistry, PhysicalChemistrystructural dynamicsmolecular-dynamicsresonance ramancarbon-monoxideligand-bindingcytochrome-cspin-statevibrational-relaxationtransient absorptionmyoglobinFemtosecond X-ray spectroscopy of haem proteinstext::journal::journal article::research article