Cysteine S−H as a Hydrogen-Bonding Probe in Proteins

Kandori, Hideki; Kinoshita, Naoko; Shichida, Yoshinori; Maeda, Akio; Needleman, Richard; Lanyi, Janos Κ.

doi:10.1021/ja980837i

Cited by 54 publications

(73 citation statements)

References 22 publications

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“…Because the OOD stretches of neat secondary alcohols, model systems of threonine, are located at 2,680 to 2,480 cm Ϫ1 (26), this result indicates that the OOD group of Thr-89 is strongly hydrogen-bonded in BR, and the hydrogen bond is further strengthened upon K formation. The lower frequency (2,466 cm Ϫ1 ) than those of neat secondary alcohols implies that the hydrogen bond of the OOD group is very strong in K. The result is consistent with the result for the SOH group of Cys-89 in the K intermediate of the T89C mutant (29). The angles of the dipole moments of the OOD stretches relative to the membrane normal were calculated to be 21°in BR and 29°in K (26).…”

Section: Methodssupporting

confidence: 83%

“…Given this unusual interaction, it was expected that the relaxation of K would be accompanied by weakening of the hydrogen bond of the OOH group of Thr-89 (26). Indeed, in an FTIR study of the T89C mutant, with a cysteine SOH as a hydrogen-bonding probe (29), the SOH stretching vibrations showed that the hydrogen bond of the SOH group at position 89 was very strong in BR, further strengthened in K, and lost in M. A broken hydrogen bond in M is also supported by x-ray crystallographic results for the M intermediate (17). However, detailed structural changes in photocycle intermediates have to be examined by polarized FTIR spectroscopy of the wild type.…”

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confidence: 99%

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Tight Asp-85–Thr-89 association during the pump switch of bacteriorhodopsin

Kandori

Yamazaki

Shichida

et al. 2001

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

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108

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Section: Methodssupporting

confidence: 83%

mentioning

confidence: 99%

Tight Asp-85–Thr-89 association during the pump switch of bacteriorhodopsin

Kandori

Yamazaki

Shichida

et al. 2001

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

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108

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“…71,72 Lower S-H stretching frequencies (down to 2477 cm −1 ) have also been observed in proteins. 73 We should note that the H-bond acceptance by the sulfur atom has a minor effect in the S-H stretching frequency of model compounds, increasing the wavenumber frequency by less than ∼5 cm −1 . 71 This experimental observation challenges the conclusions from an homology model of CrChR2 refined by QM/MM simulations, suggesting that cysteine residues showing notable vibrational changes in the S-H stretch could be H-bonded only at the sulfur atom.…”

Section: F Hydrogen-bonding Changes Of the Thiol Group Of Cysteine Rmentioning

confidence: 91%

Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1

Lórenz-Fonfrı́a

Muders

Schlesinger

et al. 2014

The Journal of Chemical Physics

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Water plays an essential role in the structure and function of proteins, particularly in the less understood class of membrane proteins. As the first of its kind, channelrhodopsin is a light-gated cation channel and paved the way for the new and vibrant field of optogenetics, where nerve cells are activated by light. Still, the molecular mechanism of channelrhodopsin is not understood. Here, we applied time-resolved FT-IR difference spectroscopy to channelrhodopsin-1 from Chlamydomonas augustae. It is shown that the ( −1 ) to moderately strongly (3300 cm −1 ) hydrogen-bonded. Changes in amide A and thiol vibrations report on global and local changes, respectively, associated with the formation of the conductive state. Future studies will aim at assigning the respective cysteine group(s) and at localizing the "dangling" water molecules within the protein, providing a better understanding of their functional relevance in CaChR1.

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“…are well isolated from other vibrations (38) and useful for monitoring their hydrogen bonding strength. Because wild-type SRII and HtrII-(1-159) both lack cysteine residues, no signal in the S-H stretching region (2580 -2525 cm Ϫ1 ) was observed in the wild-type SRII-HtrII complex.…”

Section: Infrared Spectral Changes Of Srii Upon the Formation Of The mentioning

confidence: 99%

Functional Importance of the Interhelical Hydrogen Bond between Thr204 and Tyr174 of Sensory Rhodopsin II and Its Alteration during the Signaling Process

Sudo

Furutani

Kandori

et al. 2006

Journal of Biological Chemistry

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Sensory rhodopsin II (SRII), a receptor for negative phototaxis in haloarchaea, transmits light signals through changes in protein-protein interaction with its transducer HtrII. Light-induced structural changes throughout the SRII-HtrII interface, which spans the periplasmic region, membrane-embedded domains, and cytoplasmic domains near the membrane, have been identified by several studies. Here we demonstrate by sitespecific mutagenesis and analysis of phototaxis behavior that two residues in SRII near the membrane-embedded interface (Tyr 174 on helix F and Thr 204 on helix G) are essential for signaling by the SRII-HtrII complex. These residues, which are the first in SRII shown to be required for phototaxis function, provide biological significance to the previous observation that the hydrogen bond between them is strengthened upon the formation of the earliest SRII photointermediate (SRII K ) only when SRII is complexed with HtrII. Here we report frequency changes of the S-H stretch of a cysteine substituted for SRII Thr 204 in the signaling state intermediates of the SRII photocycle, as well as an influence of HtrII on the hydrogen bond strength, supporting a direct role of the hydrogen bond in SRII-HtrII signal relay chemistry. Our results suggest that the light signal is transmitted to HtrII from the energized interhelical hydrogen bond between Thr 204 and Tyr 174 , which is located at both the retinal chromophore pocket and in helices F and G that form the membrane-embedded interaction surface to the signal-bearing second transmembrane helix of HtrII. The results argue for a critical process in signal relay occurring at this membrane interfacial region of the complex. Sensory rhodopsin II (SRII,2 also known as phoborhodopsin) is a negative phototaxis receptor in haloarchaeal prokaryotes, including Halobacterium salinarum and Natronomonas pharaonis (1-5). The SRII photoreceptor subunit forms a 2:2 complex with its transducer subunit, HtrII, in membranes and transmits light signals through changes in protein-protein interaction. The photochemical reaction cycle (6) and atomic structure of SRII (7-9) are well characterized. SRII bound to an N-terminal fragment of HtrII have provided atomic details of the two proteins' interaction surface in the periplasm and within the membrane (10), and interaction of the HtrII membrane-proximal domain with the cytoplasmic domain of the receptor has been demonstrated by fluorescent probe accessibility and Förster resonance energy transfer measurements (11), EPR of spin-labels (12), and in vitro binding of HtrII peptides to SRII (13). The signal relay mechanism from SRII to HtrII in the complex has become a focus of interest in part because of its importance to the general understanding of interaction between integral membrane proteins.The results from several different methods show that lightinduced structural changes occur all along the SRII-HtrII interface, which includes the region on the periplasmic side of the membrane, the membrane-embedded domain, and the cytoplasm...

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Cysteine S−H as a Hydrogen-Bonding Probe in Proteins

Cited by 54 publications

References 22 publications

Tight Asp-85–Thr-89 association during the pump switch of bacteriorhodopsin

Tight Asp-85–Thr-89 association during the pump switch of bacteriorhodopsin

Changes in the hydrogen-bonding strength of internal water molecules and cysteine residues in the conductive state of channelrhodopsin-1

Functional Importance of the Interhelical Hydrogen Bond between Thr204 and Tyr174 of Sensory Rhodopsin II and Its Alteration during the Signaling Process

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