Hardy B, Dubiel P, Bungay E, Rudin M, Williams C, Arthur C
Protein Sci. 2024; 33(8):e5113.
PMID: 38980168
PMC: 11232281.
DOI: 10.1002/pro.5113.
Hardy B, Hermosilla A, Chinthapalli D, Robinson C, Anderson J, Curnow P
Proc Natl Acad Sci U S A. 2023; 120(16):e2300137120.
PMID: 37036998
PMC: 10120048.
DOI: 10.1073/pnas.2300137120.
Shimada A, Hatano K, Tadehara H, Yano N, Shinzawa-Itoh K, Yamashita E
J Biol Chem. 2018; 293(38):14868-14879.
PMID: 30077971
PMC: 6153300.
DOI: 10.1074/jbc.RA118.003123.
Solomon E, Heppner D, Johnston E, Ginsbach J, Cirera J, Qayyum M
Chem Rev. 2014; 114(7):3659-853.
PMID: 24588098
PMC: 4040215.
DOI: 10.1021/cr400327t.
Chess D, Billings E, Covian R, Glancy B, French S, Taylor J
Anal Biochem. 2013; 439(2):161-72.
PMID: 23665273
PMC: 3713082.
DOI: 10.1016/j.ab.2013.04.017.
Spectral components of the α-band of cytochrome oxidase.
Kim N, Ripple M, Springett R
Biochim Biophys Acta. 2011; 1807(7):779-87.
PMID: 21420929
PMC: 3098939.
DOI: 10.1016/j.bbabio.2011.03.008.
Thermodynamic redox behavior of the heme centers in A-type heme-copper oxygen reductases: comparison between the two subfamilies.
Verissimo A, Sousa F, Baptista A, Teixeira M, Pereira M
Biophys J. 2008; 95(9):4448-55.
PMID: 18676644
PMC: 2567927.
DOI: 10.1529/biophysj.108.139493.
Carbon monoxide, reactive oxygen signaling, and oxidative stress.
Piantadosi C
Free Radic Biol Med. 2008; 45(5):562-9.
PMID: 18549826
PMC: 2570053.
DOI: 10.1016/j.freeradbiomed.2008.05.013.
Evidence for redox cooperativity between c-type hemes of MauG which is likely coupled to oxygen activation during tryptophan tryptophylquinone biosynthesis.
Li X, Feng M, Wang Y, Tachikawa H, Davidson V
Biochemistry. 2006; 45(3):821-8.
PMID: 16411758
PMC: 2565495.
DOI: 10.1021/bi052000n.
A method for dynamic spectrophotometric measurements in vivo using principal component analysis-based spectral deconvolution.
Zupancic G
Pflugers Arch. 2003; 447(1):109-19.
PMID: 12920600
DOI: 10.1007/s00424-003-1147-3.
The second derivative electronic absorption spectrum of cytochrome c oxidase in the Soret region.
Horvath M, Copeland R, Makinen M
Biophys J. 1999; 77(3):1694-711.
PMID: 10465779
PMC: 1300456.
DOI: 10.1016/S0006-3495(99)77016-5.
The role of electrostatic interactions for cytochrome c oxidase function.
Kannt A, Lancaster C, Michel H
J Bioenerg Biomembr. 1998; 30(1):81-7.
PMID: 9623809
DOI: 10.1023/a:1020563629032.
The coupling of electron transfer and proton translocation: electrostatic calculations on Paracoccus denitrificans cytochrome c oxidase.
Kannt A, Lancaster C, Michel H
Biophys J. 1998; 74(2 Pt 1):708-21.
PMID: 9533684
PMC: 1302552.
DOI: 10.1016/S0006-3495(98)73996-7.
The partially reduced species present in purified cytochrome oxidase from baker's yeast is cytochrome a.
Siedow J, Miller S, Palmer G
J Bioenerg Biomembr. 1981; 13(3-4):171-9.
PMID: 6273396
DOI: 10.1007/BF00763838.
Near-infrared magnetic and natural circular dichroism of cytochrome c oxidase.
Eglinton D, Johnson M, Thomson A, Gooding P, Greenwood C
Biochem J. 1980; 191(2):319-31.
PMID: 6263244
PMC: 1162221.
DOI: 10.1042/bj1910319.
Studies on the resolution of cytochrome oxidase.
Fry M, Green D
J Bioenerg Biomembr. 1981; 13(1-2):61-87.
PMID: 6262295
DOI: 10.1007/BF00744747.
Interactions of Ca2+ and H+ with heme A in cytochrome oxidase.
Saari H, Penttila T, Wikstrom M
J Bioenerg Biomembr. 1980; 12(3-4):325-38.
PMID: 6260769
DOI: 10.1007/BF00744692.
Interactions in cytochrome oxidase: functions and structure.
Freedman J, Chan S
J Bioenerg Biomembr. 1984; 16(2):75-100.
PMID: 6100297
DOI: 10.1007/BF00743042.
Analysis of the spectra and redox properties of pure cytochromes aa3.
Hendler R, Reddy K, Shrager R, Caughey W
Biophys J. 1986; 49(3):717-29.
PMID: 3008873
PMC: 1329518.
DOI: 10.1016/S0006-3495(86)83698-0.
The use of principal component analysis to resolve the spectra and kinetics of cytochrome c oxidase reduction by 5,10-dihydro-5-methyl phenazine.
Halaka F, Babcock G, Dye J
Biophys J. 1985; 48(2):209-19.
PMID: 2996647
PMC: 1329312.
DOI: 10.1016/S0006-3495(85)83774-7.