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H-bond network around retinal regulates the evolution of ultraviolet and violet vision.

ABSTRACT: Ancestors of vertebrates used ultraviolet vision. Some descendants preserved ultraviolet vision, whereas some others replaced it with violet vision, and then, some of avian lineages reinvented ultraviolet vision. Ultraviolet (absorption at ?360 nm) and violet (410-440 nm) sensitivities of visual pigments are known to be affected by around 20 amino acid substitutions. The present quantum mechanical/molecular mechanical calculations show that these substitutions modify a H-bond network formed by two waters and sites 86, 90, 113, 114, 118, and 295, which determines the protonation state of Schiff base linked 11-cis-retinal. A pigment is ultraviolet-sensitive when it is more stable with an unprotonated retinal (SBR) form than with its protonated analogue (PSBR) and is violet-sensitive when the PSBR form is more stable. These results establish for the first time the chemical basis of ultraviolet and violet vision in vertebrates.

SUBMITTER: Altun A

PROVIDER: S-EPMC3158842 | biostudies-literature | 2011 Aug

REPOSITORIES: biostudies-literature

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H-bond network around retinal regulates the evolution of ultraviolet and violet vision.

Altun Ahmet A Morokuma Keiji K Yokoyama Shozo S

ACS chemical biology 20110614 8

Ancestors of vertebrates used ultraviolet vision. Some descendants preserved ultraviolet vision, whereas some others replaced it with violet vision, and then, some of avian lineages reinvented ultraviolet vision. Ultraviolet (absorption at ∼360 nm) and violet (410-440 nm) sensitivities of visual pigments are known to be affected by around 20 amino acid substitutions. The present quantum mechanical/molecular mechanical calculations show that these substitutions modify a H-bond network formed by t ...[more]

PMID: 21650174

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Project description:Residues Tyr59, Gly78, Ser79, Met103, Gln107, Ile136 and Glu137 in human arsenic (+3 oxidation state) methyltransferase (hAS3MT) were deduced to form a potential hydrogen bond network around S-adenosylmethionine (SAM) from the sequence alignment between Cyanidioschyzon merolae arsenite S-adenosylmethyltransferase (CmArsM) and hAS3MT. Herein, seven mutants Y59A, G78A, S79A, M103A, Q107A, I136A and E137A were obtained. Their catalytic activities and conformations were characterized and models were built. Y59A and G78A were completely inactive. Only 7.0%, 10.6% and 13.8% inorganic arsenic (iAs) was transformed to monomethylated arsenicals (MMA) when M103A, Q107A and I136A were used as the enzyme. The Vmax (the maximal velocity of the reaction) values of M103A, Q107A, I136A and E137A were decreased to 8%, 22%, 15% and 50% of that of WT-hAS3MT, respectively. The KM(SAM) (the Michaelis constant for SAM) values of mutants M103A, I136A and E137A were 15.7, 8.9 and 5.1 fold higher than that of WT-hAS3MT, respectively, indicating that their affinities for SAM were weakened. The altered microenvironment of SAM and the reduced capacity of binding arsenic deduced from KM(As) (the Michaelis constant for iAs) value probably synergetically reduced the catalytic activity of Q107A. The catalytic activity of S79A was higher than that of WT despite of the higher KM(SAM) , suggesting that Ser79 did not impact the catalytic activity of hAS3MT. In short, residues Tyr59 and Gly78 significantly influenced the catalytic activity of hAS3MT as well as Met103, Ile136 and Glu137 because they were closely associated with SAM-binding, while residue Gln107 did not affect SAM-binding regardless of affecting the catalytic activity of hAS3MT. Modeling and our experimental results suggest that the adenine ring of SAM is sandwiched between Ile136 and Met103, the amide group of SAM is hydrogen bonded to Gly78 in hAS3MT and SAM is bonded to Tyr59 with van der Waals, cation-? and hydrogen bonding contacts.

Project description:Objective. Patients with photovoltaic subretinal implant PRIMA demonstrated letter acuity ∼0.1 logMAR worse than sampling limit for 100μm pixels (1.3 logMAR) and performed slower than healthy subjects tested with equivalently pixelated images. To explore the underlying differences between natural and prosthetic vision, we compare the fidelity of retinal response to visual and subretinal electrical stimulation through single-cell modeling and ensemble decoding.Approach. Responses of retinal ganglion cells (RGCs) to optical or electrical white noise stimulation in healthy and degenerate rat retinas were recorded via multi-electrode array. Each RGC was fit with linear-nonlinear and convolutional neural network models. To characterize RGC noise, we compared statistics of spike-triggered averages (STAs) in RGCs responding to electrical or visual stimulation of healthy and degenerate retinas. At the population level, we constructed a linear decoder to determine the accuracy of the ensemble of RGCs onN-way discrimination tasks.Main results. Although computational models can match natural visual responses well (correlation ∼0.6), they fit significantly worse to spike timings elicited by electrical stimulation of the healthy retina (correlation ∼0.15). In the degenerate retina, response to electrical stimulation is equally bad. The signal-to-noise ratio of electrical STAs in degenerate retinas matched that of the natural responses when 78 ± 6.5% of the spikes were replaced with random timing. However, the noise in RGC responses contributed minimally to errors in ensemble decoding. The determining factor in accuracy of decoding was the number of responding cells. To compensate for fewer responding cells under electrical stimulation than in natural vision, more presentations of the same stimulus are required to deliver sufficient information for image decoding.Significance. Slower-than-natural pattern identification by patients with the PRIMA implant may be explained by the lower number of electrically activated cells than in natural vision, which is compensated by a larger number of the stimulus presentations.

Dataset Information

H-bond network around retinal regulates the evolution of ultraviolet and violet vision.

Publications

H-bond network around retinal regulates the evolution of ultraviolet and violet vision.

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