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Biochemistry|February 26, 2004
The raised midpoint potential of the [2Fe2S] cluster of cytochrome bc1 is mediated by both the Qo site occupants and the head domain position of the Fe-S protein subunitJason W Cooley, Arthur G Roberts, Michael K Bowman, et al.
Biochimica Et Biophysica Acta|June 20, 2006
A functional hybrid between the cytochrome bc1 complex and its physiological membrane-anchored electron acceptor cytochrome cy in Rhodobacter capsulatusDong-Woo Lee, Yavuz Ozturk, Aygun Mamedova, et al.
Archives of Biochemistry and Biophysics|October 16, 2014
Site-directed mutagenesis of the highly perturbed copper site of auracyanin DJeremy D King, Lucas Harrington, Bryan M Lada, et al.
Biophysical Journal|October 22, 2023
Protein dynamics govern the oxyferrous state lifetime of an artificial oxygen transport proteinLei Zhang, Mia C Brown, Andrew C Mutter, et al.
The Journal of Biological Chemistry|April 2, 2011
Loss of a conserved tyrosine residue of cytochrome b induces reactive oxygen species production by cytochrome bc1Dong-Woo Lee, Nur Selamoglu, Pascal Lanciano, et al.
Biophysical Chemistry|January 21, 2014
Bilayer surface association of the pHLIP peptide promotes extensive backbone desolvation and helically-constrained structuresMia C Brown, Rauta A Yakubu, Jay Taylor, et al.
The Journal of Biological Chemistry|May 27, 2005
Uncovering the molecular mode of action of the antimalarial drug atovaquone using a bacterial systemMichael W Mather, Elisabeth Darrouzet, Maria Valkova-Valchanova, et al.
Biochemistry|October 24, 2013
Metalloproteins diversified: the auracyanins are a family of cupredoxins that stretch the spectral and redox limits of blue copper proteinsJeremy D King, Chelsea L McIntosh, Christopher M Halsey, et al.
Biochemistry|April 8, 2014
Role of bilayer characteristics on the structural fate of aβ(1-40) and aβ(25-40)Jian Xiong, Carol A Roach, Olayinka O Oshokoya, et al.
Biophysical Journal|April 12, 2018
Unwinding of the Substrate Transmembrane Helix in Intramembrane ProteolysisMia C Brown, Alaa Abdine, Jose Chavez, et al.
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