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. 2021 Dec 6;6(50):34912–34919. doi: 10.1021/acsomega.1c05564

Table 1. Absorption Spectra of Oxidized [M(III)], Reduced [M(II)], and Oxygen-Bound [M(II)-O2] forms of Fe-AfGcHK and Co-AfGcHK. M = Fe or Coa.

  M(III) M(II) M(II)-O2
Heme Proteins
Fe-AfGcHK 411, 539 432, 562 348, 413, 545, 580
  His/OH– His His/O2
  6cLS 5cHS 6cLS
Mbb 358, 414, 542, 582e 434, 556 348, 418, 543, 581
  His/OH– His His/O2
  6cLS 5cHS 6cLS
Hbb 410, 540, 575e 430, 555 344, 415, 541, 577
  His/OH– His His/O2
  6cLS 5cHS 6cLS
Cobalt-Substituted Proteins
Co-AfGcHK 358, 427, 538, 569 398, 557 358, 427, 540, 574
  His/OH– His His/O2
  6cLS 5cLS 6cLS
CoHRPc 427, 538, 572e 401, 553 424, 535, 567
  His/OH– His His/O2
  6cLS 5cLS 6cLS
CoMbd not reported 406, 558 426, 539, 577
    His His/O2
    5cLS 6cLS
CoHbd not reported 402, 552 428, 538, 571
    His His/O2
    5cLS 6cLS
a

Corresponding spectra of other relevant native and cobalt-substituted heme proteins are shown as a reference. Proposed coordination structures are also presented. 6cLS, 6-coordinated low-spin; 5cHS, 5-coordinated high-spin; 5cLS, 5-coordinated low-spin.

b

Reference (2).

c

Reference (17).

d

Reference (18).

e

For comparison with AfGcHK, alkaline OH– forms are shown.