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1 s two iron atoms, but does not behave like a hemerythrin.
2 ts involved in reversible binding of O(2) to hemerythrin.
3 center, probably similar to the one found in hemerythrin.
4 typical of mu-oxo-bridged di-iron containing hemerythrins.
5 e tunnel" distinct from that in invertebrate hemerythrins.
6 , lines the O(2)-binding pocket in all known hemerythrins.
7 r stabilization found in dioxygen binding to hemerythrin, albeit with reversed polarity, suggests tha
8 lectron transfer (i.e., the OH/oxo bridge in hemerythrin), and simulations of the binding of O2 in a
10 length, while Mn catalase and Mn-substituted hemerythrin appear to have a larger RMS bond length devi
11 3d areas for Mn catalase and Mn-substituted hemerythrin are larger, suggesting that one or both of t
13 al characterization of the ligand-responsive hemerythrin domain provides insights into the mechanisms
14 FBXL5 contains an iron- and oxygen-binding hemerythrin domain that acted as a ligand-dependent regu
15 stic link between iron sensing via the FBXL5 hemerythrin domain, IRP2 regulation, and cellular respon
17 the Fe enzymes ribonucleotide reductase and hemerythrin have been determined using X-ray absorption
18 contributors to microaerophily in C. jejuni; hemerythrins help prevent enzyme damage microaerobically
21 haliana), BRUTUS (BTS), which contains three hemerythrin (HHE) domains and a Really Interesting New G
22 sults are compared to our earlier studies of Hemerythrin (Hr) and a common theme emerges where the sp
25 ng the stable diiron-mononitrosyl complex of hemerythrin, Hr(NO), for which we observe a nu(NO) at 16
29 atomic structure of the FBXL5 N terminus, a hemerythrin-like alpha-helical bundle fold not previousl
32 esulfovibrio vulgaris (Hildenborough), has a hemerythrin-like domain, DcrH-Hr, at its C terminus.
33 bioinformatic analyses suggest that multiple hemerythrin-like protein coding sequences might have bee
35 conclude that it is a member of a subset of hemerythrin-like proteins exclusive to mycobacteria, wit
37 y, we have systematically analyzed all three hemerythrin-like proteins in M. smegmatis and our result
39 d by lateral gene transfer and the number of hemerythrin-like proteins varies amongst different speci
42 o recombinant proteins, Phascolopsis gouldii hemerythrin (Pg-Hr) and Desulfovibrio vulgaris rubreryth
43 inuclear iron active site similar to that in hemerythrin, ribonucleotide reductase, and methane monoo
44 ype found in soluble diiron proteins such as hemerythrin, ribonucleotide reductase, methane monooxyge
45 XAFS data for Mn catalase and Mn-substituted hemerythrin show two distinct Mn-nearest neighbor shells
46 Leu-98 in recombinant Phascolopsis gouldii hemerythrin, was mutated to several other residues of va
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