scholarly journals 2P098 Heme binding site in Rhodnius prolixus α-glucosidase promoting the heme crystallization(02. Heme proteins,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S175
Author(s):  
Shotaro Kaku ◽  
Keisuke Nakatani ◽  
Haruto Ishikawa ◽  
Yasuhisa Mizutani
Keyword(s):  
Binding Site ◽  
Heme Proteins ◽  
Rhodnius Prolixus ◽  
Heme Binding

scholarly journals The CytochromecFold Can Be Attained from a Compact Apo State by Occupancy of a Nascent Heme Binding Site

2001 ◽  
Vol 276 (49) ◽  
pp. 45813-45817 ◽  
Author(s):  
Rachel Wain ◽  
Thelma A. Pertinhez ◽  
Esther J. Tomlinson ◽  
Lin Hong ◽  
Christopher M. Dobson ◽  
...  
Keyword(s):  
Binding Site ◽  
Heme Binding ◽  
Apo State

scholarly journals Mechanistic insights into heme-mediated transcriptional regulation via a bacterial manganese-binding iron regulator, iron response regulator (Irr)

2020 ◽  
Vol 295 (32) ◽  
pp. 11316-11325
Author(s):  
Dayeon Nam ◽  
Yuki Matsumoto ◽  
Takeshi Uchida ◽  
Mark R. O'Brian ◽  
Koichiro Ishimori
Keyword(s):  
Binding Site ◽  
Fluorescence Anisotropy ◽  
Response Regulator ◽  
Binding Activity ◽  
Control Element ◽  
Heme Binding ◽  
Cluster Region ◽  
Ice Binding ◽  
Iron Response Regulator ◽  
Ice Complex

The transcription factor iron response regulator (Irr) is a key regulator of iron homeostasis in the nitrogen-fixating bacterium Bradyrhizobium japonicum. Irr acts by binding to target genes, including the iron control element (ICE), and is degraded in response to heme binding. Here, we examined this binding activity using fluorescence anisotropy with a 6-carboxyfluorescein-labeled ICE-like oligomer (FAM-ICE). In the presence of Mn2+, Irr addition increased the fluorescence anisotropy, corresponding to formation of the Irr–ICE complex. The addition of EDTA to the Irr–ICE complex reduced fluorescence anisotropy, but fluorescence was recovered after Mn2+ addition, indicating that Mn2+ binding is a prerequisite for complex formation. Binding activity toward ICE was lost upon introduction of substitutions in a His-cluster region of Irr, revealing that Mn2+ binds to this region. We observed that the His-cluster region is also the heme binding site; results from fluorescence anisotropy and electrophoretic mobility shift analyses disclosed that the addition of a half-equivalent of heme dissociates Irr from ICE, likely because of Mn2+ release due to heme binding. We hypothesized that heme binding to another heme binding site, Cys-29, would also inhibit the formation of the Irr–ICE complex because it is proximal to the ICE binding site, which was supported by the loss of ICE binding activity in a Cys-29–mutated Irr. These results indicate that Irr requires Mn2+ binding to form the Irr–ICE complex and that the addition of heme dissociates Irr from ICE by replacing Mn2+ with heme or by heme binding to Cys-29.

scholarly journals Highly malleable haem-binding site of the haemoprotein HasA permits stable accommodation of bulky tetraphenylporphycenes

RSC Advances ◽  
2019 ◽  
Vol 9 (32) ◽  
pp. 18697-18702 ◽  
Author(s):  
Erika Sakakibara ◽  
Yuma Shisaka ◽  
Hiroki Onoda ◽  
Daiki Koga ◽  
Ning Xu ◽  
...  
Keyword(s):  
Binding Site ◽  
Heme Binding ◽  
Flexible Loops

Bulky metallo-tetraphenylporphycene was successfully incorporated into haemophore HasA which have flexible loops surrounding heme-binding site.

Oxygen diffusion near the heme binding site of horseradish peroxidase

1991 ◽  
Vol 178 (1) ◽  
pp. 104-109 ◽  
Author(s):  
Victor Vargas ◽  
Juan E. Brunet ◽  
David M. Jameson
Keyword(s):  
Horseradish Peroxidase ◽  
Binding Site ◽  
Oxygen Diffusion ◽  
Heme Binding

The role of eicosanoids on Rhodnius heme-binding protein (RHBP) endocytosis by Rhodnius prolixus ovaries

2002 ◽  
Vol 32 (5) ◽  
pp. 537-545 ◽  
Author(s):  
Marcelo N Medeiros ◽  
Danielle M.P Oliveira ◽  
Gabriela O Paiva-Silva ◽  
Mário A.C Silva-Neto ◽  
Alexandre Romeiro ◽  
...  
Keyword(s):  
Binding Protein ◽  
Rhodnius Prolixus ◽  
Heme Binding ◽  
Heme Binding Protein
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