Raw material exploitation strategies on the flint mining site of Spiennes (Hainaut, Belgium)

The flint mines of Spiennes (Hainaut Province, Belgium) are among the most important mining sites in Europe as evidenced by the huge extension of the site and its very long duration of occupation, probably covering a period between 4350 and 2300 BCE. What explains such a spectacular achievement? The paper first explores the geological constraints but also the social and material conditions that made possible such a continuity of mining activities. The site of Spiennes offers both extremely rich flint resources and a specific geographical configuration that made the discovery and the exploitation of the deposit relatively easy in the Neolithic. The paper next focuses on deducing the mining strategies implemented to extract good quality raw materials on basis of both stratigraphical evidence and the flint productions in direct relation with the mines. The mining strategies variability from a synchronic and a diachronic point of view as well as the knapping techniques implemented will be analysed. These are then put into perspective with what is known of the social context in which the mining activities took place. At the turn of the 5th and the 4th millennium BCE a permanent settlement was built near the mining site. As the Michelsberg populations who exploited the mines in Spiennes were first and foremost farmers, this leads us to propose a tentative hypothesis about the seasonality of the mining activities. Living close to a hugely rich flint deposit, these farmers were able to develop sometimes complex mining techniques to reach specific seams, deemed adequate for the production of standardised axeheads and blades. Century-old traditions, group specialisation in mining and knapping and close social control of flint resources allowed the mines to dominate the raw material supply of the Mons Basin for centuries

Detailed studies of the subpicosecond kinetics in the primary electron transfer of reaction centers of Rhodopseudomonas viridis

The primary, light-induced charge separation in reaction centers of Rhodopseudomonas viridis is investigated with femtosecond time resolution. The absorption changes after direct excitation of the primary donor P at 955 nm are investigated in the time range from 100 fs to 600 ps. The experimental data, taken at various probing wavelengths, reveal one subpicosecond and two picosecond time constants: 0.65 ± 0.2 ps, 3.5 ± 0.4 ps, and 200 ± 20 ps. The previously undetected 0.65 ps kinetics can be observed clearly in the spectral range of the Qx and Qy transitions of the monomeric bacteriochlorophylls. The experimental data support the idea that the accessory bacteriochlorophyll B A participates in the electron-transfer process. Reference

Temperature dependence of the primary electron transfer in photosynthetic reaction centers from Rhodobacter sphaeroides

The primary electron transfer (ET) in reaction centers (RC) of Rhodobacter sphaeroides is investigated as a function of temperature with femtosecond time resolution. For temperatures from 300 to 25 K the ET to the bacteriopheophytin is characterized by a biphasic time dependence. The two time constants of τ1=3.5±0.4 ps and τ2=1.2±0.3 ps at T=300 K decrease continously with temperature to values of τ1=1.4±0.3 ps and τ2=0.3±0.15 ps at 25 K. The experimental results indicate that the ET is not thermally activated and that the same ET mechanisms are active at room and low temperatures. All observations are readily rationalized by a two-step ET model with the monomeric bacteriochlorophyll as a real electron carrier

Modified bacterial reaction centers

Pigments of borohydride-treated reaction centers of Rhodobacter sphaeroides R 26 and Rhodopseudomonas viridis were analyzed by HPLC with polychromatic detection. In both species, pigment composition and contents were unchanged. Reaction centers from Rhodobacter sphaeroides R26 were prepared in which bacteriochlorophylls (BA,B) and bacteriopheophytins (HA,B) were exchanged with their potential borohydride products reduced at C-31. [3-Hydroxyethyl]-BChl a exchanges selectively into the BA,B pockets, and 31-OH-BPh a to the HA,B pockets. Stable reaction centers are obtained in both cases. A comparison of the absorption and circular dichroism spectra of reaction centers after exchange with 31-OH pigments, and of borohydride-modified reaction centers, reveal distinct differences. It is concluded that during borohydride reduction none of the pigments is chemically modified or extracted from the reaction centers

Weak temperature dependence of P (+) H A (-) recombination in mutant Rhodobacter sphaeroides reaction centers

International audienceIn contrast with findings on the wild-type Rhodobacter sphaeroides reaction center, biexponential P (+) H A (-) → PH A charge recombination is shown to be weakly dependent on temperature between 78 and 298 K in three variants with single amino acids exchanged in the vicinity of primary electron acceptors. These mutated reaction centers have diverse overall kinetics of charge recombination, spanning an average lifetime from ~2 to ~20 ns. Despite these differences a protein relaxation model applied previously to wild-type reaction centers was successfully used to relate the observed kinetics to the temporal evolution of the free energy level of the state P (+) H A (-) relative to P (+) B A (-) . We conclude that the observed variety in the kinetics of charge recombination, together with their weak temperature dependence, is caused by a combination of factors that are each affected to a different extent by the point mutations in a particular mutant complex. These are as follows: (1) the initial free energy gap between the states P (+) B A (-) and P (+) H A (-) , (2) the intrinsic rate of P (+) B A (-) → PB A charge recombination, and (3) the rate of protein relaxation in response to the appearance of the charge separated states. In the case of a mutant which displays rapid P (+) H A (-) recombination (ELL), most of this recombination occurs in an unrelaxed protein in which P (+) B A (-) and P (+) H A (-) are almost isoenergetic. In contrast, in a mutant in which P (+) H A (-) recombination is relatively slow (GML), most of the recombination occurs in a relaxed protein in which P (+) H A (-) is much lower in energy than P (+) H A (-) . The weak temperature dependence in the ELL reaction center and a YLH mutant was modeled in two ways: (1) by assuming that the initial P (+) B A (-) and P (+) H A (-) states in an unrelaxed protein are isoenergetic, whereas the final free energy gap between these states following the protein relaxation is large (~250 meV or more), independent of temperature and (2) by assuming that the initial and final free energy gaps between P (+) B A (-) and P (+) H A (-) are moderate and temperature dependent. In the case of the GML mutant, it was concluded that the free energy gap between P (+) B A (-) and P (+) H A (-) is large at all times