Joseph Katigbak1, Yong Zhang. 1. Department of Chemistry, Chemical Biology, and Biomedical Engineering, Stevens Institute of Technology, Castle Point on Hudson Hoboken, NJ 07030, Unites States.
Abstract
Fur protein plays key roles in regulating numerous genes in bacteria and is essential for intracellular iron concentration regulation. However, atomic level pictures of the iron binding site and its functional mechanism remain to be established. Here we present results of the first quantum chemical investigation of various first- and second-shell models and experimental Mössbauer data of E. Coli Fur, including 1) the first robust evidence that site 2 is the Fe binding site with a 3His/2Glu ligand set, being the first case in non-heme proteins, with computed Mössbauer data in excellent accord with experiment; 2) the first discovery of a conservative hydrogen bonding interaction in the iron binding site based on X-ray and homology structures; 3) the first atomic level hypothesis of active site reorganization upon iron concentration increase, triggering the conformational change needed for its function. These results shall facilitate structural and functional studies of Fur family proteins.
n class="Chemical">Fur protein plays key roles in regulating numerous genes in bacteria and is essential for intracellular iron concentration regulation. However, atomic level pictures of the iron binding site and its functional mechanism remain to be established. Here we present results of the first quantum chemical investigation of various first- and second-shell models and experimental Mössbauer data of E. ColiFur, including 1) the first robust evidence that site 2 is the Fe binding site with a 3His/2Glu ligand set, being the first case in non-heme proteins, with computed Mössbauer data in excellent accord with experiment; 2) the first discovery of a conservative hydrogen bonding interaction in the iron binding site based on X-ray and homology structures; 3) the first atomic level hypothesis of active site reorganization upon iron concentration increase, triggering the conformational change needed for its function. These results shall facilitate structural and functional studies of Fur family proteins.
Authors: Dorothea K Thompson; Alexander S Beliaev; Carol S Giometti; Sandra L Tollaksen; Tripti Khare; Douglas P Lies; Kenneth H Nealson; Hanjo Lim; John Yates; Craig C Brandt; James M Tiedje; Jizhong Zhou Journal: Appl Environ Microbiol Date: 2002-02 Impact factor: 4.792
Authors: A Gonzalez de Peredo; C Saint-Pierre; A Adrait; L Jacquamet; J M Latour; I Michaud-Soret; E Forest Journal: Biochemistry Date: 1999-06-29 Impact factor: 3.162
Authors: A Adrait; L Jacquamet; L Le Pape; A Gonzalez de Peredo; D Aberdam; J L Hazemann; J M Latour; I Michaud-Soret Journal: Biochemistry Date: 1999-05-11 Impact factor: 3.162
Authors: Victor J Torres; Ahmed S Attia; William J Mason; M Indriati Hood; Brian D Corbin; Federico C Beasley; Kelsi L Anderson; Devin L Stauff; W Hayes McDonald; Lisa J Zimmerman; David B Friedman; David E Heinrichs; Paul M Dunman; Eric P Skaar Journal: Infect Immun Date: 2010-01-25 Impact factor: 3.441
Authors: Ryan A Barker; Jerrell Tisnado; Lisa A Lambert; Astrid Gärdes; Mary W Carrano; Paul N Carrano; Christopher Gillian; Carl J Carrano Journal: Biometals Date: 2014-12-21 Impact factor: 2.949
Authors: Laura Botello-Morte; Silvia Pellicer; Violeta C Sein-Echaluce; Lellys M Contreras; José Luis Neira; Olga Abián; Adrián Velázquez-Campoy; María Luisa Peleato; María F Fillat; María Teresa Bes Journal: Antioxid Redox Signal Date: 2015-10-09 Impact factor: 8.401
Authors: Rahul L Khade; Wenchao Fan; Yan Ling; Liu Yang; Eric Oldfield; Yong Zhang Journal: Angew Chem Int Ed Engl Date: 2014-06-06 Impact factor: 15.336