Is the heme pocket region modulated by disulfide-bridge formation in fish and amphibian neuroglobins as in humans?

Leuven, Wendy Van; Cuypers, Bert; Desmet, Filip; Giordano, Daniela; Verde, Cinzia; Moëns, Luc; Doorslaer, Sabine Van; Dewilde, Sylvia

doi:10.1016/j.bbapap.2013.01.042

Cited by 7 publications

(1 citation statement)

References 28 publications

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“…The redox state of the Cys(CD5)46/Cys(D5)55 residue pair affects the reactivity of human Ngb (Hamdane et al, 2003). However, this mechanism does not apply to (i) murine Ngb, which contains a Gly residue at position (CD5)46 instead of Cys (Vallone et al, 2004a), and (ii) amphibian and fish Ngbs differing in the positions of Cys residues (Van Leuven et al, 2013). In human Ngb, the reduction of the Cys(CD5)46-Cys(D5)55 disulfide bridge and the mutation of these Cys residues reduce the dissociation rate of His(E7)64 (i.e., k−H) from the six-coordinate heme-Fe atom by about oneorder of magnitude (i.e., from 7.0 s −1 to 6.0 × 10 −1 s −1 ) and decrease the value of the equilibrium constant for His(E7)64 binding to the sixth-coordination position of the heme-Fe atom (i.e., KH) by about one-order of magnitude (i.e., from 2.8 × 10 2 to 3.9 × 10 3 ).…”

Section: The Redox State Of the Cys(cd5)46/cys(d5)55 Residue Pairmentioning

confidence: 99%

Neuroglobin: From structure to function in health and disease

Ascenzi

Masi

Leboffe

et al. 2016

Molecular Aspects of Medicine

145

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Section: The Redox State Of the Cys(cd5)46/cys(d5)55 Residue Pairmentioning

confidence: 99%

Neuroglobin: From structure to function in health and disease

Ascenzi

Masi

Leboffe

et al. 2016

Molecular Aspects of Medicine

145

View full text Add to dashboard Cite

Engineering Human Neuroglobin into a Cytochrome c‐Like Protein with a Single Thioether Bond in Non‐native State

et al. 2022

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A double mutant of human H64M/V71C neuroglobin (Ngb) was engineered, which formed a single thioether bond as that in atypical cytochrome c, whereas the heme distal Met64 was oxidized to both sulfoxide (SO-Met) and sulfone (SO 2 -Met). By contrast, no Cys-heme cross-link was formed in V71C Ngb with His64/His96 coordination, as shown by the X-ray crystal structure, which indicates that an open distal site facilitates the activation of heme iron for structural modifications.

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Neuroglobin Expression in the Brain: a Story of Tissue Homeostasis Preservation

2018

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After its discovery in 2000, the notion grew that neuroglobin, a neuronal specific heme protein, is involved in cytoprotection. To date, neuroglobin levels have been positively correlated with a beneficial outcome in a plethora of neurotoxic insults, e.g., ischemic and traumatic brain injuries and Alzheimer's disease. The first part of this review goes further into these changes of neuroglobin expression upon different neuronal insults as well as the underlying regulation. In the second part, we shed light on the mechanisms by which neuroglobin contributes to neuroprotection, being (i) the scavenging and detoxification of reactive oxygen/nitrogen species, (ii) the augmentation of the threshold for apoptosis initiation, (iii) its contribution to an anti-inflammatory milieu, and (iv) tissue regeneration. We also consider different neuroglobin models to address as yet unanswered questions. Based on the recent findings and progress in the field, we invigorate the avenues of neuroglobin in neurological ailments to increase in the coming years.

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Is the heme pocket region modulated by disulfide-bridge formation in fish and amphibian neuroglobins as in humans?

Cited by 7 publications

References 28 publications

Neuroglobin: From structure to function in health and disease

Neuroglobin: From structure to function in health and disease

Engineering Human Neuroglobin into a Cytochrome c‐Like Protein with a Single Thioether Bond in Non‐native State

Neuroglobin Expression in the Brain: a Story of Tissue Homeostasis Preservation

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