NDLI: Structural model and spectroscopic characteristics of the FMO antenna protein from the aerobic chlorophototroph, Candidatus Chloracidobacterium thermophilum

Content Provider	PubMed Central
Author	Wen, Jianzhong Tsukatani, Yusuke Cui, Weidong Zhang, Hao Gross, Michael L. Bryant, Donald A. Blankenship, Robert E.
Copyright Year	2010
Abstract	The Fenna–Matthews–Olson protein (FMO) binds seven or eight bacteriochlorophyll a (BChl a) molecules and is an important model antenna system for understanding pigment-protein interactions and mechanistic aspects of photosynthetic light harvesting. FMO proteins of green sulfur bacteria (Chlorobiales) have been extensively studied using a wide range of spectroscopic and theoretical approaches because of their stability, the spectral resolution of their pigments, their water-soluble nature, and the availability of high-resolution structural data. We obtained new structural and spectroscopic insights by studying the FMO protein from the recently discovered, aerobic phototrophic acidobacterium, Candidatus Chloracidobacterium thermophilum. Native C. thermophilum FMO is a trimer according to both analytical gel filtration and native-electrospray mass spectrometry. Furthermore, the mass of intact FMO trimer is consistent with the presence of 21–24 BChl a in each. Homology modeling of the C. thermophilum FMO was performed by using the structure of the FMO protein from Chlorobaculum tepidum as a template. C. thermophilum FMO differs from C. tepidum FMO in two distinct regions: the baseplate, CsmA-binding region and a region that is proposed to bind the reaction center subunit, PscA. C. thermophilum FMO has two fluorescence emission peaks at room temperature but only one at 77 K. Temperature-dependent fluorescence spectroscopy showed that the two room-temperature emission peaks result from two excited-state BChl a populations that have identical fluorescence lifetimes. Modeling of the data suggests that the two populations contain 1–2 BChl and 5–6 BChl a molecules and that thermal equilibrium effects modulate the relative population of the two emitting states.
Related Links	http://dx.doi.org/10.1016/j.bbabio.2010.09.008
Ending Page	164
Page Count	8
Starting Page	157
File Format	PDF
ISSN	00052728
Journal	Biochimica et biophysica acta
Issue Number	1
Volume Number	1807
Language	English
Publisher Date	2011-01-01
Access Restriction	Open
Subject Keyword	Biophysics Cell Biology Biochemistry Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Biophysics

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Characterization of the FMO protein from the aerobic chlorophototroph, Candidatus Chloracidobacterium thermophilum

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