H2020Индивидуална стипендия2017–2019

Act-EPR · Active Resonator Development for nano-EPR of single crystal proteins

„Хоризонт 2020“ — Действия „Мария Склодовска-Кюри“

Период: 2017-05-01 → 2019-06-23
Финансиране от ЕС: 171 461 €
Участници: 1
Схема: MSCA-IF-EF-ST

Линиите свързват координатора с партньорите.

Накратко на български

Ензимите, като например хидрогеназата, се изследват чрез нов метод за анализ на електронната структура на техните активни центрове. Това помага за разбирането на природните катализатори, което е основа за създаването на системи за съхранение на чиста енергия.

Този кратък обзор е генериран от изкуствен интелект

Кратко обяснение, генерирано от езиков модел по текста на CORDIS. Оригиналът е по-долу.

Резултати накратко

Active Resonator Development for nano-EPR of single crystal proteins

In order to keep up with societal challenges of the 21st century, we must devise sustainable ways to efficiently store and retrieve energy. What better way to solve these problems than to look to nature? Fully understanding the catalytic mechanism of enzymes provides a basis for synthetic models designed for practical applications. For example, hydrogenase based and inspired systems provide an interesting route to advance towards a “hydrogen economy” and the future of clean energy. We employ Electron Paramagnetic Resonance (EPR) to study the paramagnetic states of hydrogenases and obtain information on electronic and geometrical structure of their active site. Single crystal experiments are the ultimate method in determining the full-tensor magnetic interactions of the enzyme. However, the application of single-crystal EPR to metallo-proteins is severely limited by the small crystals sizes which are less than 27 nL in volume. In order to make single crystal EPR available as tool to study redox and metallo-proteins, a breakthrough in absolute sensitivity is necessary. The development of a self-resonant micro-helix (Fig02) with a factor up to 28 in signal-to-noise improvement has met this goal. It is now possible to perform advanced pulse EPR experiments on protein single-crystals with dimensions that are typical for X-ray crystallography diffraction. This has a direct impact on biophysical and biochemical basic science initiatives. For the first time, a full g-tensor is proposed for the Hox state of [FeFe]-hydrogenase (Fig01). The protein single-crystal had dimensions of 0.3 x 0.1 x 0.1 mm3 (3 nL) and each trace took only 8 minutes to collect with a signal-to-noise ratio of 290. The g-tensor proposed here is directly measured and refines the previously proposed g-tensors which relied heavily on assumptions. Act-EPR is at the core of basic science research in order to better understand both the structure and function of enzymes. Not only does the understanding of such enzymes advance our scientific knowledge, but it provides a path for drug discovery and bioengineering mimics of enzymes for industrial purposes.

Текст от CORDIS, на английски · Данни: CORDIS, © Европейски съюз

Цел на проекта

In order to keep up with societal challenges of the 21st century, we must devise sustainable ways to efficiently store and retrieve energy from hydrogen. This “hydrogen economy” is one path for the future of clean energy. Nature’s solution to this challenge is a branch of enzymes called hydrogenases which typically use an organometallic active-site to reversibly split molecular hydrogen to hydrogen-ions and energy, in the form of electrons. Here, we choose to focus on [FeFe]-hydrogenase due to its high catalytic behavior. To understand these metallo-enzymes we must be able to study the enzymes grown as a single crystal. Single crystal protein Electron Paramagnetic Resonance (EPR) experiments are the ultimate method to study the paramagnetic states of hydrogenases and obtain the full magnetic interactions reflecting the electronic structure of the active site. Ultimately the catalytic activity of the hydrogenase can be understood by relating the information of the magnetic principal axes to the known protein structure of the enzyme. However, the application of single-crystal EPR is severely limited by the small crystals sizes that are usually available (sub-nanoliter to nanoliter volumes). The Key Enabling Technologies outlined in this fellowship have the potential to increase the sensitivity of EPR by a factor of 30 through the application of highly innovative concepts based on planar micro-resonators (PMR). This technology provides the sensitivity needed for the applicant to be the first to study single crystals of the [FeFe]-hydrogenase enzyme with EPR and advance the “hydrogen economy”.

Оригинален текст от CORDIS (на английски).

Участници

MAX-PLANCK-GESELLSCHAFT ZUR FORDERUNG DER WISSENSCHAFTEN EV · MUNCHENКоординаторГермания