James A Fee
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Explore the profile of James A Fee including associated specialties, affiliations and a list of published articles.
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34
Citations
647
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Recent Articles
1.
Funatogawa C, Li Y, Chen Y, McDonald W, Szundi I, Fee J, et al.
Biochemistry
. 2016 Dec;
56(1):107-119.
PMID: 28026953
Knowledge of the role of conserved residues in the ligand channel of heme-copper oxidases is critical for understanding how the protein scaffold modulates the function of these enzymes. In this...
2.
Egawa T, Haber J, Fee J, Yeh S, Rousseau D
J Phys Chem B
. 2015 Jun;
119(27):8509-20.
PMID: 26056844
In heme-copper oxidases, the correlation curve between the iron-CO and C-O stretching vibrational modes (ν(Fe-CO) and ν(C-O), respectively) is anomalous as compared to the correlation in other heme proteins. To...
3.
Noodleman L, Han Du W, Fee J, Gotz A, Walker R
Inorg Chem
. 2014 Jun;
53(13):6458-72.
PMID: 24960612
After a summary of the problem of coupling electron and proton transfer to proton pumping in cytochrome c oxidase, we present the results of our earlier and recent density functional...
4.
McDonald W, Funatogawa C, Li Y, Chen Y, Szundi I, Fee J, et al.
Biochemistry
. 2014 Jun;
53(27):4467-75.
PMID: 24937405
Knowing how the protein environment modulates ligand pathways and redox centers in the respiratory heme-copper oxidases is fundamental for understanding the relationship between the structure and function of these enzymes....
5.
McDonald W, Funatogawa C, Li Y, Szundi I, Chen Y, Fee J, et al.
Biochemistry
. 2013 Jan;
52(4):640-52.
PMID: 23282175
Knowledge of the structure and dynamics of the ligand channel(s) in heme-copper oxidases is critical for understanding how the protein environment modulates the functions of these enzymes. Using photolabile NO...
6.
Luna V, Fee J, Deniz A, Stout C
Biochemistry
. 2012 May;
51(23):4669-76.
PMID: 22607023
We use a form of "freeze-trap, kinetic crystallography" to explore the migration of Xe atoms away from the dinuclear heme a(3)/Cu(B) center in Thermus thermophilus cytochrome ba(3) oxidase. This enzyme...
7.
Chang H, Choi S, Vakkasoglu A, Chen Y, Hemp J, Fee J, et al.
Proc Natl Acad Sci U S A
. 2012 Mar;
109(14):5259-64.
PMID: 22431640
The heme-copper oxygen reductases are redox-driven proton pumps. In the current work, the effects of mutations in a proposed exit pathway for pumped protons are examined in the ba(3)-type oxygen...
8.
Neehaul Y, Chen Y, Werner C, Fee J, Ludwig B, Hellwig P
Biochim Biophys Acta
. 2012 Mar;
1817(10):1950-4.
PMID: 22402225
The hydrophobically guided complex formation between the Cu(A) fragment from Thermus thermophilus ba(3) terminal oxidase and its electron transfer substrate, cytochrome c(552), was investigated electrochemically. In the presence of the...
9.
Liu B, Zhang Y, Sage J, Soltis S, Doukov T, Chen Y, et al.
Biochim Biophys Acta
. 2012 Jan;
1817(4):658-65.
PMID: 22226917
The purpose of the work was to provide a crystallographic demonstration of the venerable idea that CO photolyzed from ferrous heme-a(3) moves to the nearby cuprous ion in the cytochrome...
10.
Egawa T, Chen Y, Fee J, Yeh S, Rousseau D
Biochim Biophys Acta
. 2011 Dec;
1817(4):666-71.
PMID: 22138627
Cytochrome ba(3) (ba(3)) of Thermus thermophilus (T. thermophilus) is a member of the heme-copper oxidase family, which has a binuclear catalytic center comprised of a heme (heme a(3)) and a...