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1 0 (PA1673), which we named mhr for microoxic hemerythrin.
2 ts involved in reversible binding of O(2) to hemerythrin.
3 s two iron atoms, but does not behave like a hemerythrin.
4 center, probably similar to the one found in hemerythrin.
5 typical of mu-oxo-bridged di-iron containing hemerythrins.
6 e tunnel" distinct from that in invertebrate hemerythrins.
7 , lines the O(2)-binding pocket in all known hemerythrins.
8 r stabilization found in dioxygen binding to hemerythrin, albeit with reversed polarity, suggests tha
9 lectron transfer (i.e., the OH/oxo bridge in hemerythrin), and simulations of the binding of O2 in a
10 yl carrier protein desaturase, rubrerythrin, hemerythrin, and the ferritins.
11 length, while Mn catalase and Mn-substituted hemerythrin appear to have a larger RMS bond length devi
12  3d areas for Mn catalase and Mn-substituted hemerythrin are larger, suggesting that one or both of t
13 ple of a regulatory function for a bacterial hemerythrin (Bhr) domain is reported.
14 al characterization of the ligand-responsive hemerythrin domain provides insights into the mechanisms
15   FBXL5 contains an iron- and oxygen-binding hemerythrin domain that acted as a ligand-dependent regu
16 stic link between iron sensing via the FBXL5 hemerythrin domain, IRP2 regulation, and cellular respon
17 e wild type protein, and several of the L98X hemerythrins formed stable oxy adducts.
18  the Fe enzymes ribonucleotide reductase and hemerythrin have been determined using X-ray absorption
19 contributors to microaerophily in C. jejuni; hemerythrins help prevent enzyme damage microaerobically
20  enzyme activity and identify a role for the hemerythrin HerA (Cj0241).
21                                      Another hemerythrin (HerB; Cj1224) also plays a protective role.
22 haliana), BRUTUS (BTS), which contains three hemerythrin (HHE) domains and a Really Interesting New G
23 sults are compared to our earlier studies of Hemerythrin (Hr) and a common theme emerges where the sp
24  is negatively regulated by highly conserved hemerythrin (Hr) E3 ubiquitin ligases exemplified by Ara
25                                              Hemerythrin (Hr) is an O(2)-carrying protein found in so
26 of a C-terminal soluble domain homologous to hemerythrin (Hr) proteins and domains.
27 ng the stable diiron-mononitrosyl complex of hemerythrin, Hr(NO), for which we observe a nu(NO) at 16
28                                              Hemerythrins (Hrs) and myohemerythrins (Mhrs) are nonhem
29 thrin (Dv-Rr), have been examined as well as hemerythrin isolated from Lingula reevii (Lr-Hr).
30                             FBXL5 contains a hemerythrin-like (Hr) domain at its N terminus that medi
31  atomic structure of the FBXL5 N terminus, a hemerythrin-like alpha-helical bundle fold not previousl
32 rs, two rubredoxin Fe(Cys)(4) centers, and a hemerythrin-like diiron site.
33 n in a process that required an iron-binding hemerythrin-like domain in its N terminus.
34                                          The hemerythrin-like domain of F-box and leucine-rich repeat
35 llular iron environment based on a mammalian hemerythrin-like domain, acting as an iron-dependent lig
36 esulfovibrio vulgaris (Hildenborough), has a hemerythrin-like domain, DcrH-Hr, at its C terminus.
37 bioinformatic analyses suggest that multiple hemerythrin-like protein coding sequences might have bee
38                                          The hemerythrin-like protein from Mycobacterium kansasii (Mk
39                                              Hemerythrin-like proteins (HLPs) are broadly distributed
40                                              Hemerythrin-like proteins are oxygen-carrying non-heme d
41  conclude that it is a member of a subset of hemerythrin-like proteins exclusive to mycobacteria, wit
42  Rv2633c is a member of a distinct subset of hemerythrin-like proteins exclusive to mycobacteria.
43 iron nitric oxide reductases (FNORs) and the hemerythrin-like proteins from mycobacteria (HLPs), are
44 y, we have systematically analyzed all three hemerythrin-like proteins in M. smegmatis and our result
45 ghts into the evolutionary divergence of the hemerythrin-like proteins in M. smegmatis.
46 d by lateral gene transfer and the number of hemerythrin-like proteins varies amongst different speci
47       Mycobacterium smegmatis contains three hemerythrin-like proteins, MSMEG_3312, MSMEG_2415 and MS
48 ce of an HHE cation-binding domain common in hemerythrin-like proteins.
49 o recombinant proteins, Phascolopsis gouldii hemerythrin (Pg-Hr) and Desulfovibrio vulgaris rubreryth
50 inuclear iron active site similar to that in hemerythrin, ribonucleotide reductase, and methane monoo
51 ype found in soluble diiron proteins such as hemerythrin, ribonucleotide reductase, methane monooxyge
52 XAFS data for Mn catalase and Mn-substituted hemerythrin show two distinct Mn-nearest neighbor shells
53   Leu-98 in recombinant Phascolopsis gouldii hemerythrin, was mutated to several other residues of va
54 oxygen-binding proteins, such as globins and hemerythrins, which arose in the ancestor of bilaterian