Structure and function of haemoglobins

Gell, David A.

doi:10.1016/j.bcmd.2017.10.006

Cited by 166 publications

(131 citation statements)

References 550 publications

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“…Mb is a monomeric protein consisting of 154 amino acids, structurally related to haemoglobin, and endowed with oxygen transport and storage functions . The structure of Mb was characterized over 60 years ago and comprises eight α‐helices labelled A to H .…”

Section: Introductionmentioning

confidence: 99%

“…Mb is a monomeric protein consisting of 154 amino acids, structurally related to haemoglobin, and endowed with oxygen transport and storage functions. [17] The structure of Mb was characterized over 60 years ago and comprises eight α-helices labelled A to H. [18] Mb is able to bind oxygen as well as a variety of small molecules via its haem chromophore, such as water, carbon monoxide, nitrogen monoxide, cyanide, and azide ions. [19,20] The capability of Mb of binding more bulky ligands than the above-mentioned gases, for example, imidazole, has been demonstrated as well.…”

Section: Introductionmentioning

confidence: 99%

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Resonance Raman optical activity of the imidazole–Myoglobin complex: Titrating enhancement

Sgammato

Herrebout

Johannessen

2019

J Raman Spectroscopy

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Resonance Raman optical activity (rROA) is a very powerful chiroptical technique for the investigation of bioactive protein cofactors in native conformation, due to its sensitivity towards any tiny conformational changes occurring at the chromophore. Twelve years ago, the rROA spectrum of myoglobin was published for the first time, revealing the strong potential of the technique for the selective study of the haem moiety. In this contribution, the use of rROA has been extended to the ligand binding properties of myoglobin via a combined approach of resonance Raman/ROA and ultraviolet‐visible absorption/electronic circular dichroism. The treatment of myoglobin with molar excess of imidazole in aqueous solution has led to the formation of a brilliant red pigment, known as imidazolylmet‐myoglobin, and revealed an interesting evolution of the visible Q bands, with the appearance of Qα at 534 nm. The use of the laser excitation of 532 nm, in resonance with the S0–S1 electronic transition (Q bands) of the sample, induced the selective Raman and ROA enhancement of certain haem vibrational modes, in a concentration‐dependent manner. Here, we highlight the sensitivity of rROA spectroscopy towards conformational changes of the haem chromophore upon interaction with the exogenous molecule, allowing us to distinguish between the bound and unligated form of the globin, a fundamental step towards the full understanding of the haem‐ligand binding process.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Resonance Raman optical activity of the imidazole–Myoglobin complex: Titrating enhancement

Sgammato

Herrebout

Johannessen

2019

J Raman Spectroscopy

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“…They arose early in evolution, and it has been proposed that their primordial functions were those of enzymes or sensors of molecular oxygen (O 2 ) [2,3]. In all functional globins, an invariant His residue forms a coordinate bond to the central Fe atom at the proximal site of the heme cofactor, whereas substrates bind to the sixth coordination site of the Fe ion, located at the distal site [4]. Hbs known to date belong to either of two structural sub-classes and are phylogenetically divided into three large families.…”

Section: Introductionmentioning

confidence: 99%

“…The ubiquity of globins and the diversity of their primary sequences reflect their diverse functions, of which the well-studied storage and transport of O 2 is suggested to be a rather recent evolutionary invention. Hbs are known today to bind additional ligands such as hydrogen sulfide, and to catalyze enzymatic reactions, such as the O 2 -dependent nitric oxide (NO) conversion to nitrate, through a reaction termed NO dioxygenation, or nitrite reduction to NO [3,4]. Although most Hbs studied in vitro can bind various ligands, such as O 2 , NO, carbon monoxide (CO) or cyanide (CN -), and perform diverse enzymatic reactions, individual proteins are tuned towards certain functions through variations of the heme-Fe reactivity or its accessibility, modulated by the protein.…”

Section: Introductionmentioning

confidence: 99%

“…The dissociation of a ligand is mostly related to the strength of the bond between the heme-Fe and the substrate, which can be influenced by proximal and distal effects. Proximal effects mainly work through the coordinating HisF8 residue, which affects the electronic structure and the mobility of the heme-Fe [4]. The distal side exerts influence on substrate binding mostly by the presence or absence of H-bond networks that stabilize the ligand [24,25].…”

Section: Introductionmentioning

confidence: 99%

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Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions

et al. 2020

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Hemoglobins (Hbs) utilize heme b as a cofactor and are found in all kingdoms of life. The current knowledge reveals an enormous variability of Hb primary sequences, resulting in topological, biochemical and physiological individuality. As Hbs appear to modulate their reactivities through specific combinations of structural features, predicting the characteristics of a given Hb is still hardly possible. The unicellular green alga Chlamydomonas reinhardtii contains 12 genes encoding diverse Hbs of the truncated lineage, several of which possess extended N-or C-termini of unknown function. Studies on some of the Chlamydomonas Hbs revealed yet unpredictable structural and biochemical variations, which, along with a different expression of their genes, suggest diverse physiological roles. Chlamydomonas thus represents a promising system to analyze the diversification of Hb structure, biochemistry and physiology. Here, we report the crystal structure, resolved to 1.75 Å, of the heme-binding domain of cyanomet THB11 (Cre16.g662750), one of the pentacoordinate algal Hbs, which offer a free Fe-coordination site in the reduced state. The overall fold of THB11 is conserved, but individual features such as a kink in helix E, a tilted heme plane and a clustering of methionine residues at a putative tunnel exit appear to be unique. Both N-and C-termini promote the formation of oligomer mixtures, and the absence of the C terminus results in reduced nitrite reduction rates. This work widens the structural and biochemical knowledge on the 2/2Hb family and suggests that the N-and C-terminal extensions of the Chlamydomonas 2/2Hbs modulate their reactivity by intermolecular interactions.

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Erythrocyte‐Inspired Functional Materials for Biomedical Applications

et al. 2022

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Erythrocytes are the most abundant cells in the blood. As the results of long‐term natural selection, their specific biconcave discoid morphology and cellular composition are responsible for gaining excellent biological performance. Inspired by the intrinsic features of erythrocytes, various artificial biomaterials emerge and find broad prospects in biomedical applications such as therapeutic delivery, bioimaging, and tissue engineering. Here, a comprehensive review from the fabrication to the applications of erythrocyte‐inspired functional materials is given. After summarizing the biomaterials mimicking the biological functions of erythrocytes, the synthesis strategies of particles with erythrocyte‐inspired morphologies are presented. The emphasis is on practical biomedical applications of these bioinspired functional materials. The perspectives for the future possibilities of the advanced erythrocyte‐inspired biomaterials are also discussed. It is hoped that the summary of existing studies can inspire researchers to develop novel biomaterials; thus, accelerating the progress of these biomaterials toward clinical biomedical applications.

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Structure and function of haemoglobins

Cited by 166 publications

References 550 publications

Resonance Raman optical activity of the imidazole–Myoglobin complex: Titrating enhancement

Resonance Raman optical activity of the imidazole–Myoglobin complex: Titrating enhancement

Distinctive structural properties of THB11, a pentacoordinate Chlamydomonas reinhardtii truncated hemoglobin with N- and C-terminal extensions

Erythrocyte‐Inspired Functional Materials for Biomedical Applications

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