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. 2011 Aug 18;286(41):35522–35534. doi: 10.1074/jbc.M111.274811

TABLE 1.

Absorption spectra of the Fe(III), Fe(II), Fe(II)-O2, and Fe(II)-CO complexes of wild-type and mutant AfGcHK

Corresponding spectra of other heme-based oxygen sensor enzymes and SWMb are shown as the reference. Proposed coordination structures are presented in parentheses. 6cLS, 6-coordinated low spin; 5cHS, 5-coordinated high spin; 6cHS, 6-coordinated high spin.

Proteins Fe(III) Fe(II) Fe(II)-O2 Fe(II)-CO
AfGcHK
    WT 411, 538 (6cLS) 431, 559 (5cHS) 413, 545, 580 (6cLS) 420, 541, 565 (6cLS)
    Y45F 411, 535 (6cLS) 430, 555 (5cHS) 414, 546, 579 (6cLS) 420, 541, 563 (6cLS)
    Y45L 410, 534 (6cLS) 431, 564 (5cHS) 415, 548, 578 (6cLS) 421, 541, 565 (6cLS)
    Y45W 410, 534 (6cLS) 431, 558 (5cHS) 414, 547, 580 (6cLS) 420, 543, 565 (6cLS)
    H99A No heme absorption
    H183A 411, 543 (6cLS) 432, 561 (5cHS) 413, 545, 580 (6cLS) 421, 541, 565 (6cLS)
YddVa 394, 506, 651 (5cHS) 432, 560 (5cHS) 413, 542, 578 (6cLS) 420, 539, 566 (6cLS)
HemAT-Bsb 402, 505, 640 (6cHS) 431, 563 (5cHS) 414, 543, 578 (6cLS) 422, 543, 567 (6cLS)
SWMbc 410, 505, 635 (6cHS) 434, 556 (5cHS) 418, 543, 581 (6cLS) 423, 542, 579 (6cLS)
EcDOSd 417, 530, 562 (6cLS) 428, 532, 563 (6cLS) 417, 542, 578 (6cLS) 424, 542, 578 (6cLS)
BjFixLe 395, 509, 645 (5cHS) 437, 556 (5cHS) 419, 545, 562 (6cLS) 427, 548, 560 (6cLS)

a Ref. 28.

b Ref. 30.

c Ref. 37.

d Refs. 22 and 53.

e Ref. 46.