ArticleBiophysical journal2010
Probing the role of the internal disulfide bond in regulating conformational dynamics in neuroglobin.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 31 citations in OpenAlex.
- Neuroglobin: A New Player in the Gut-Brain Axis.International journal of molecular sciences · 2026Review
- Electrochemical and Spectroscopic Characterization of Co-Neuroglobin: A Bioelectrocatalyst for HInorganic chemistry · 2025Article
- Hydrogen peroxide induces heme degradation and protein aggregation in human neuroglobin: roles of the disulfide bridge and hydrogen-bonding in the distal heme cavity.The FEBS journal · 2023Article
- Structural and (Pseudo-)Enzymatic Properties of Neuroglobin: Its Possible Role in Neuroprotection.Cells · 2021Review
- Enhancement of protein stability by an additional disulfide bond designed in human neuroglobin.RSC advances · 2019Article
- Peroxidase activation of cytoglobin by anionic phospholipids: Mechanisms and consequences.Biochimica et biophysica acta · 2016Article
- A possible mechanism for redox control of human neuroglobin activity.Journal of chemical information and modeling · 2014Article
- Heme orientation modulates histidine dissociation and ligand binding kinetics in the hexacoordinated human neuroglobin.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this report, we demonstrate that the internal disulfide bridge in human neuroglobin modulates structural changes associated with ligand photo-dissociation from the heme active site. This is evident from time-resolved photothermal studies of CO photo-dissociation, which reveal a 13.4+/-0.9 mL mol(-1) volume expansion upon ligand photo-release from human neuroglobin, whereas the CO dissociation from rat neuroglobin leads to a significantly smaller volume change (DeltaV=4.6+/-0.3 mL mol(-1)). Reduction of the internal disulfide bond in human neuroglobin leads to conformational changes (reflected by DeltaV) nearly identical to those observed for rat Ngb. Our data favor the hypothesis that the disulfide bond between Cys46 and Cys55 modulates the functioning of human neuroglobin.
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Registered trials
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