Chapter 2 Primary photochemical events in the rhodopsin molecule

Yoshizawa, Tôru; Kandori, Hideki

doi:10.1016/0278-4327(91)90023-u

Cited by 17 publications

(11 citation statements)

References 69 publications

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“…Since photoreceptor IOS onset time was shorter than ERG awave onset time, it suggests that the photoreceptor originated from the early stage of phototransduction before the hyperpolarization of the retinal photoreceptor, which generates ERG a-wave. According to Yoshizawa and Kandori, 44 the time required for rhodopsin to absorb photons and become enzymatically active is around 1 ms. Figure 6(d) shows that, when averaged, photoreceptor IOS could be observed at ∼0.4 ms, and this confirmed that photoreceptor IOS originated from early phototransduction.…”

Section: Discussionmentioning

confidence: 99%

In vivooptical coherence tomography of stimulus-evoked intrinsic optical signals in mouse retinas

Wang

Yao

2016

J. Biomed. Opt

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Abstract. Intrinsic optical signal (IOS) imaging promises a noninvasive method for advanced study and diagnosis of eye diseases. Before pursuing clinical applications, it is essential to understand anatomic and physiological sources of retinal IOSs and to establish the relationship between IOS distortions and eye diseases. The purpose of this study was designed to demonstrate the feasibility of in vivo IOS imaging of mouse models. A high spatiotemporal resolution spectral domain optical coherence tomography (SD-OCT) was employed for depth-resolved retinal imaging. A custom-designed animal holder equipped with ear bar and bite bar was used to minimize eye movements. Dynamic OCT imaging revealed rapid IOS from the photoreceptor's outer segment immediately after the stimulation delivery, and slow IOS changes were observed from inner retinal layers.Comparative photoreceptor IOS and electroretinography recordings suggested that the fast photoreceptor IOS may be attributed to the early stage of phototransduction before the hyperpolarization of retinal photoreceptor.

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Section: Discussionmentioning

confidence: 99%

In vivooptical coherence tomography of stimulus-evoked intrinsic optical signals in mouse retinas

Wang

Yao

2016

J. Biomed. Opt

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“…For electric field effect, De Dios and Oldfield (34) showed that weak electric field effects (␣ 1͞r 3 ) are the dominant factors, which obviated the need to invoke secondorder van der Waals interactions (␣ 1͞r 6 ). Such a shift is a clear indication of effect of neighboring atoms on a 19 F-label and is distance dependent.…”

Section: Background Informationmentioning

confidence: 99%

“…The structure of the primary photoproduct of rhodopsin is still largely unknown. For many years bathorhodopsin ( max ϭ 535 nm) was considered the primary photoproduct of rhodopsin (1,19). In the 1980s the Kyoto group (20,21) identified an earlier intermediate in their time-resolved studies, named photorhodopsin ( max ϭ 570 nm).…”

Section: Background Informationmentioning

confidence: 99%

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The molecular basis for the high photosensitivity of rhodopsin

Liu

Colmenares

2003

Proc. Natl. Acad. Sci. U.S.A.

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Based on structural information derived from the F NMR data of labeled rhodopsins, rhodopsin crystal structure, and excited-state properties of model polyenes, we propose a molecular mechanism that accounts specifically for the causes of the well-known enhanced photoreactivity of rhodopsin (increased rates and quantum yield of isomerization). Rhodopsin is a heptahelical membrane protein responsible for scotopic vision. It is a photo-receptor protein activated by the 11-cis-retinal (1) (Structure 1) chromophore covalently bonded to Lys-296 through a protonated Schiff base (PSB) linkage. The photoisomerization of the chromophore initiates the vision process (1). The pigment is known to possess unusually high photochemical reactivity. For example, its quantum yield of isomerization is 0.65 (2, 3) (a recently refined value from the long accepted number of 0.67; ref. 4), more than two times higher than that of the same chromophore in solution (0.24, 0.22) (5, 6). The rate of isomerization is also much faster in protein (146 fsec) (7) than in solution (1-2 psec) (8). In this article, we propose a detailed molecular model accounting for the unusual protein assistance to the isomerization process. Background Information

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“…6 However, its predicted stereochemical consequence of one-photon-two-bond isomerization did not agree with the one-bond isomerization of rhodopsin. 7 Sub-sequently, the Hula-twist (HT) volume conserving (turning over of one C-H unit) mechanism of isomerization was proposed. 4,8 Its predicted stereochemical consequence of si-Dedicated to the memory of the late Professor Ho Tong-Ing.…”

Section: Introductionmentioning

confidence: 99%

A Re‐investigation of Low Temperature Photochemistry of 11‐cis‐retinal Mechanism of Photoisomerization

Yang

Liu

2006

J Chinese Chemical Soc

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Photoisomerization of 11‐cis‐retinal in an organic glass, believed to originate from the 12‐s‐cis con‐former, gives an unstable primary photoproduct(s). The implication of simultaneous single and double bond isomerization is only consistent with an HT mechanism of isomerization. Relation of this isomerization process in the rigid medium of organic glasses with that reported for the same 11‐cis‐retinyl chromophore confined within the binding cavity of rhodopsin (as revealed by reported X‐ray crystal structural study) is discussed.

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Chapter 2 Primary photochemical events in the rhodopsin molecule

Cited by 17 publications

References 69 publications

In vivooptical coherence tomography of stimulus-evoked intrinsic optical signals in mouse retinas

In vivooptical coherence tomography of stimulus-evoked intrinsic optical signals in mouse retinas

The molecular basis for the high photosensitivity of rhodopsin

A Re‐investigation of Low Temperature Photochemistry of 11‐cis‐retinal Mechanism of Photoisomerization

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