Additional file 1 of Expansion and diversity of caspases in Mytilus coruscus contribute to larval metamorphosis and environmental adaptation

Supplementary Material

The development of cobalt phosphide co-catalysts on BiVO4 photoanodes to improve H2O2 production

Photoanodic hydrogen peroxide (H2O2) production via water oxidation is limited by low yields and poor selectivity. Herein, four variations of cobalt phosphides, including pristine CoP and Co2P crystals, and two mixed-phase cobalt phosphides (CoP/Co2P) with different ratios, were applied as co-catalysts on the BiVO4 (BVO) photoanode to improve H2O2 production. The optimal yield and selectivity were approximately 9.6 µmol?h-1?cm-2 and 25.2 % at a voltage bias of 1.7 V vs reversible hydrogen electrode (VRHE) under sunlight illumination, respectively. This performance is approximately 1.8 times that of pristine BVO photoanode. The roles of the Co and P sites were investigated. In particular, the Co site promotes the breaking of one HO bond in water to form OH• radicals, which is the rate-determining step in H2O2 production. The P site plays an important role in the desorption of H2O2 formed from the catalyst, which is responsible for the recovery of fresh catalytic sites. Among the four samples, Co2P exhibited the best performance for H2O2 production because it had the highest rate of OH• formation owing to its improved accumulation property. This study offers a rational design strategy for co-catalysts for photoanodic H2O2 production

MOESM5 of Massive expansion and diversity of nicotinic acetylcholine receptors in lophotrochozoans

Additional file 5: Figure S5. Expression of six nAChR genes in gills of C. gigas under different environmental conditions (data from Zhang et al. 2012). a Seven days at 5–25 °C or 12 h at 30 and 35 °C; b Seven days under different salinities; and c Air exposure for different durations

MOESM3 of Massive expansion and diversity of nicotinic acetylcholine receptors in lophotrochozoans

Additional file 3: Figure S3. Multi-alignment of alpha nAChR genes from H. sapiens

MOESM4 of Massive expansion and diversity of nicotinic acetylcholine receptors in lophotrochozoans

Additional file 4: Figure S4. Sequence diversity at and around ACh binding sites in 33 nAChR genes of C. gigas with the sites conserved. Sequences marked by the red underline is the Cys-loop. Amino acids in green boxes are ACh binding sites. Hsa, H. sapiens; Tma, Torpedo marmorata. Genes in purple are nAChRs with completely conserved principal binding sites

MOESM7 of Massive expansion and diversity of nicotinic acetylcholine receptors in lophotrochozoans

Additional file 7: Table S1. Expression of nAChR genes (RPKM > 1) in different organs and at different development stages in C. gigas and P. f. martensii

MOESM2 of Massive expansion and diversity of nicotinic acetylcholine receptors in lophotrochozoans

Additional file 2: Figure S2. Multi-alignment of Cys-loop of nAChR genes from C. gigas and H. sapiens

MOESM1 of Massive expansion and diversity of nicotinic acetylcholine receptors in lophotrochozoans

Additional file 1: Figure S1. Extron-intron structure of nAChR genes from H. sapiens

MOESM6 of Massive expansion and diversity of nicotinic acetylcholine receptors in lophotrochozoans

Additional file 6: Figure S6. Expression of nAChR genes in gills of C. gigas in response to infection by pathogens. Left, expression of 3 nAChRs at different times after Vibrio (V. anguillarum, V. tubiashii, V. aestuarianus, V. alginolyticus) challenge (data from Zhang et al. 2015); Right, expression of 3 nAChRs at different times after Ostreid herpesvirus 1-μVar challenge (data from He et al. 2015). Y-axes is expression relative to Time 0

The 18 signatured genes in the 18-gene de-correlated model.

<p>The 18 signatured genes in the 18-gene de-correlated model.</p